The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase.
Identifieur interne : 000227 ( Main/Exploration ); précédent : 000226; suivant : 000228The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase.
Auteurs : Lindsay N. Petersen [Afrique du Sud] ; Sandra Marineo ; Salvatore Mandalà ; Faezah Davids ; Bryan T. Sewell ; Robert A. IngleSource :
- Plant physiology [ 1532-2548 ] ; 2010.
Descripteurs français
- KwdFr :
- ADN bactérien (génétique), ADN des plantes (génétique), Arabidopsis (enzymologie), Arabidopsis (génétique), Histidine (biosynthèse), Histidinol (métabolisme), Histidinol-phosphatase (génétique), Histidinol-phosphatase (métabolisme), Modèles moléculaires (MeSH), Mutagenèse par insertion (MeSH), Mutation (MeSH), Phosphorylation (MeSH), Phylogenèse (MeSH), Protéines d'Arabidopsis (génétique), Protéines d'Arabidopsis (métabolisme), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Régulation de l'expression des gènes végétaux (MeSH), Structure tertiaire des protéines (MeSH), Test de complémentation (MeSH).
- MESH :
- biosynthèse : Histidine.
- enzymologie : Arabidopsis.
- génétique : ADN bactérien, ADN des plantes, Arabidopsis, Histidinol-phosphatase, Protéines d'Arabidopsis, Protéines de fusion recombinantes.
- métabolisme : Histidinol, Histidinol-phosphatase, Protéines d'Arabidopsis, Protéines de fusion recombinantes.
- Modèles moléculaires, Mutagenèse par insertion, Mutation, Phosphorylation, Phylogenèse, Régulation de l'expression des gènes végétaux, Structure tertiaire des protéines, Test de complémentation.
English descriptors
- KwdEn :
- Arabidopsis (enzymology), Arabidopsis (genetics), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), DNA, Bacterial (genetics), DNA, Plant (genetics), Gene Expression Regulation, Plant (MeSH), Genetic Complementation Test (MeSH), Histidine (biosynthesis), Histidinol (metabolism), Histidinol-Phosphatase (genetics), Histidinol-Phosphatase (metabolism), Models, Molecular (MeSH), Mutagenesis, Insertional (MeSH), Mutation (MeSH), Phosphorylation (MeSH), Phylogeny (MeSH), Protein Structure, Tertiary (MeSH), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism).
- MESH :
- chemical , biosynthesis : Histidine.
- chemical , genetics : Arabidopsis Proteins, DNA, Bacterial, DNA, Plant, Histidinol-Phosphatase, Recombinant Fusion Proteins.
- enzymology : Arabidopsis.
- genetics : Arabidopsis.
- chemical , metabolism : Arabidopsis Proteins, Histidinol, Histidinol-Phosphatase, Recombinant Fusion Proteins.
- Gene Expression Regulation, Plant, Genetic Complementation Test, Models, Molecular, Mutagenesis, Insertional, Mutation, Phosphorylation, Phylogeny, Protein Structure, Tertiary.
Abstract
Histidine (His) plays a critical role in plant growth and development, both as one of the standard amino acids in proteins, and as a metal-binding ligand. While genes encoding seven of the eight enzymes in the pathway of His biosynthesis have been characterized from a number of plant species, the identity of the enzyme catalyzing the dephosphorylation of histidinol-phosphate to histidinol has remained elusive. Recently, members of a novel family of histidinol-phosphate phosphatase proteins, displaying significant sequence similarity to known myoinositol monophosphatases (IMPs) have been identified from several Actinobacteria. Here we demonstrate that a member of the IMP family from Arabidopsis (Arabidopsis thaliana), myoinositol monophosphatase-like2 (IMPL2; encoded by At4g39120), has histidinol-phosphate phosphatase activity. Heterologous expression of IMPL2, but not the related IMPL1 protein, was sufficient to rescue the His auxotrophy of a Streptomyces coelicolor hisN mutant. Homozygous null impl2 Arabidopsis mutants displayed embryonic lethality, which could be rescued by supplying plants heterozygous for null impl2 alleles with His. In common with the previously characterized HISN genes from Arabidopsis, IMPL2 was expressed in all plant tissues and throughout development, and an IMPL2:green fluorescent protein fusion protein was targeted to the plastid, where His biosynthesis occurs in plants. Our data demonstrate that IMPL2 is the HISN7 gene product, and suggest a lack of genetic redundancy at this metabolic step in Arabidopsis, which is characteristic of the His biosynthetic pathway.
DOI: 10.1104/pp.109.150805
PubMed: 20023146
PubMed Central: PMC2832243
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase.</title><author><name sortKey="Petersen, Lindsay N" sort="Petersen, Lindsay N" uniqKey="Petersen L" first="Lindsay N" last="Petersen">Lindsay N. Petersen</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>Department of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701</wicri:regionArea><wicri:noRegion>Rondebosch 7701</wicri:noRegion></affiliation></author><author><name sortKey="Marineo, Sandra" sort="Marineo, Sandra" uniqKey="Marineo S" first="Sandra" last="Marineo">Sandra Marineo</name></author><author><name sortKey="Mandala, Salvatore" sort="Mandala, Salvatore" uniqKey="Mandala S" first="Salvatore" last="Mandalà">Salvatore Mandalà</name></author><author><name sortKey="Davids, Faezah" sort="Davids, Faezah" uniqKey="Davids F" first="Faezah" last="Davids">Faezah Davids</name></author><author><name sortKey="Sewell, Bryan T" sort="Sewell, Bryan T" uniqKey="Sewell B" first="Bryan T" last="Sewell">Bryan T. Sewell</name></author><author><name sortKey="Ingle, Robert A" sort="Ingle, Robert A" uniqKey="Ingle R" first="Robert A" last="Ingle">Robert A. Ingle</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20023146</idno><idno type="pmid">20023146</idno><idno type="doi">10.1104/pp.109.150805</idno><idno type="pmc">PMC2832243</idno><idno type="wicri:Area/Main/Corpus">000234</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000234</idno><idno type="wicri:Area/Main/Curation">000234</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000234</idno><idno type="wicri:Area/Main/Exploration">000234</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase.</title><author><name sortKey="Petersen, Lindsay N" sort="Petersen, Lindsay N" uniqKey="Petersen L" first="Lindsay N" last="Petersen">Lindsay N. Petersen</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>Department of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701</wicri:regionArea><wicri:noRegion>Rondebosch 7701</wicri:noRegion></affiliation></author><author><name sortKey="Marineo, Sandra" sort="Marineo, Sandra" uniqKey="Marineo S" first="Sandra" last="Marineo">Sandra Marineo</name></author><author><name sortKey="Mandala, Salvatore" sort="Mandala, Salvatore" uniqKey="Mandala S" first="Salvatore" last="Mandalà">Salvatore Mandalà</name></author><author><name sortKey="Davids, Faezah" sort="Davids, Faezah" uniqKey="Davids F" first="Faezah" last="Davids">Faezah Davids</name></author><author><name sortKey="Sewell, Bryan T" sort="Sewell, Bryan T" uniqKey="Sewell B" first="Bryan T" last="Sewell">Bryan T. Sewell</name></author><author><name sortKey="Ingle, Robert A" sort="Ingle, Robert A" uniqKey="Ingle R" first="Robert A" last="Ingle">Robert A. Ingle</name></author></analytic><series><title level="j">Plant physiology</title><idno type="eISSN">1532-2548</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (enzymology)</term><term>Arabidopsis (genetics)</term><term>Arabidopsis Proteins (genetics)</term><term>Arabidopsis Proteins (metabolism)</term><term>DNA, Bacterial (genetics)</term><term>DNA, Plant (genetics)</term><term>Gene Expression Regulation, Plant (MeSH)</term><term>Genetic Complementation Test (MeSH)</term><term>Histidine (biosynthesis)</term><term>Histidinol (metabolism)</term><term>Histidinol-Phosphatase (genetics)</term><term>Histidinol-Phosphatase (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Mutagenesis, Insertional (MeSH)</term><term>Mutation (MeSH)</term><term>Phosphorylation (MeSH)</term><term>Phylogeny (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN bactérien (génétique)</term><term>ADN des plantes (génétique)</term><term>Arabidopsis (enzymologie)</term><term>Arabidopsis (génétique)</term><term>Histidine (biosynthèse)</term><term>Histidinol (métabolisme)</term><term>Histidinol-phosphatase (génétique)</term><term>Histidinol-phosphatase (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Mutagenèse par insertion (MeSH)</term><term>Mutation (MeSH)</term><term>Phosphorylation (MeSH)</term><term>Phylogenèse (MeSH)</term><term>Protéines d'Arabidopsis (génétique)</term><term>Protéines d'Arabidopsis (métabolisme)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Régulation de l'expression des gènes végétaux (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Test de complémentation (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Histidine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Arabidopsis Proteins</term><term>DNA, Bacterial</term><term>DNA, Plant</term><term>Histidinol-Phosphatase</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Histidine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN bactérien</term><term>ADN des plantes</term><term>Arabidopsis</term><term>Histidinol-phosphatase</term><term>Protéines d'Arabidopsis</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arabidopsis Proteins</term><term>Histidinol</term><term>Histidinol-Phosphatase</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Histidinol</term><term>Histidinol-phosphatase</term><term>Protéines d'Arabidopsis</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation, Plant</term><term>Genetic Complementation Test</term><term>Models, Molecular</term><term>Mutagenesis, Insertional</term><term>Mutation</term><term>Phosphorylation</term><term>Phylogeny</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Modèles moléculaires</term><term>Mutagenèse par insertion</term><term>Mutation</term><term>Phosphorylation</term><term>Phylogenèse</term><term>Régulation de l'expression des gènes végétaux</term><term>Structure tertiaire des protéines</term><term>Test de complémentation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Histidine (His) plays a critical role in plant growth and development, both as one of the standard amino acids in proteins, and as a metal-binding ligand. While genes encoding seven of the eight enzymes in the pathway of His biosynthesis have been characterized from a number of plant species, the identity of the enzyme catalyzing the dephosphorylation of histidinol-phosphate to histidinol has remained elusive. Recently, members of a novel family of histidinol-phosphate phosphatase proteins, displaying significant sequence similarity to known myoinositol monophosphatases (IMPs) have been identified from several Actinobacteria. Here we demonstrate that a member of the IMP family from Arabidopsis (Arabidopsis thaliana), myoinositol monophosphatase-like2 (IMPL2; encoded by At4g39120), has histidinol-phosphate phosphatase activity. Heterologous expression of IMPL2, but not the related IMPL1 protein, was sufficient to rescue the His auxotrophy of a Streptomyces coelicolor hisN mutant. Homozygous null impl2 Arabidopsis mutants displayed embryonic lethality, which could be rescued by supplying plants heterozygous for null impl2 alleles with His. In common with the previously characterized HISN genes from Arabidopsis, IMPL2 was expressed in all plant tissues and throughout development, and an IMPL2:green fluorescent protein fusion protein was targeted to the plastid, where His biosynthesis occurs in plants. Our data demonstrate that IMPL2 is the HISN7 gene product, and suggest a lack of genetic redundancy at this metabolic step in Arabidopsis, which is characteristic of the His biosynthetic pathway.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20023146</PMID><DateCompleted><Year>2010</Year><Month>06</Month><Day>16</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1532-2548</ISSN><JournalIssue CitedMedium="Internet"><Volume>152</Volume><Issue>3</Issue><PubDate><Year>2010</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase.</ArticleTitle><Pagination><MedlinePgn>1186-96</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1104/pp.109.150805</ELocationID><Abstract><AbstractText>Histidine (His) plays a critical role in plant growth and development, both as one of the standard amino acids in proteins, and as a metal-binding ligand. While genes encoding seven of the eight enzymes in the pathway of His biosynthesis have been characterized from a number of plant species, the identity of the enzyme catalyzing the dephosphorylation of histidinol-phosphate to histidinol has remained elusive. Recently, members of a novel family of histidinol-phosphate phosphatase proteins, displaying significant sequence similarity to known myoinositol monophosphatases (IMPs) have been identified from several Actinobacteria. Here we demonstrate that a member of the IMP family from Arabidopsis (Arabidopsis thaliana), myoinositol monophosphatase-like2 (IMPL2; encoded by At4g39120), has histidinol-phosphate phosphatase activity. Heterologous expression of IMPL2, but not the related IMPL1 protein, was sufficient to rescue the His auxotrophy of a Streptomyces coelicolor hisN mutant. Homozygous null impl2 Arabidopsis mutants displayed embryonic lethality, which could be rescued by supplying plants heterozygous for null impl2 alleles with His. In common with the previously characterized HISN genes from Arabidopsis, IMPL2 was expressed in all plant tissues and throughout development, and an IMPL2:green fluorescent protein fusion protein was targeted to the plastid, where His biosynthesis occurs in plants. Our data demonstrate that IMPL2 is the HISN7 gene product, and suggest a lack of genetic redundancy at this metabolic step in Arabidopsis, which is characteristic of the His biosynthetic pathway.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Petersen</LastName><ForeName>Lindsay N</ForeName><Initials>LN</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Marineo</LastName><ForeName>Sandra</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Mandalà</LastName><ForeName>Salvatore</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Davids</LastName><ForeName>Faezah</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Sewell</LastName><ForeName>Bryan T</ForeName><Initials>BT</Initials></Author><Author ValidYN="Y"><LastName>Ingle</LastName><ForeName>Robert A</ForeName><Initials>RA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>12</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004269">DNA, Bacterial</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018744">DNA, Plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C036483">T-DNA</NameOfSubstance></Chemical><Chemical><RegistryNumber>4QD397987E</RegistryNumber><NameOfSubstance UI="D006639">Histidine</NameOfSubstance></Chemical><Chemical><RegistryNumber>501-28-0</RegistryNumber><NameOfSubstance UI="D006641">Histidinol</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.15</RegistryNumber><NameOfSubstance UI="D006642">Histidinol-Phosphatase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004269" MajorTopicYN="N">DNA, Bacterial</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018744" MajorTopicYN="N">DNA, Plant</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005816" MajorTopicYN="N">Genetic Complementation Test</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006639" MajorTopicYN="N">Histidine</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006641" MajorTopicYN="N">Histidinol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006642" MajorTopicYN="N">Histidinol-Phosphatase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016254" MajorTopicYN="N">Mutagenesis, Insertional</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>12</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>12</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>6</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20023146</ArticleId><ArticleId IdType="pii">pp.109.150805</ArticleId><ArticleId IdType="doi">10.1104/pp.109.150805</ArticleId><ArticleId IdType="pmc">PMC2832243</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Nov 30;101(48):16976-81</Citation><ArticleIdList><ArticleId IdType="pubmed">15550539</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2009 Jun;150(2):951-61</Citation><ArticleIdList><ArticleId IdType="pubmed">19339506</ArticleId></ArticleIdList></Reference><Reference><Citation>Protein Sci. 1999 May;8(5):978-84</Citation><ArticleIdList><ArticleId IdType="pubmed">10338008</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1995 May 23;92(11):4997-5000</Citation><ArticleIdList><ArticleId IdType="pubmed">7761437</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Biochim Pol. 1971;18(3):299-307</Citation><ArticleIdList><ArticleId IdType="pubmed">4331571</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1998 May 29;428(3):229-34</Citation><ArticleIdList><ArticleId IdType="pubmed">9654139</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Protoc. 2007;2(7):1565-72</Citation><ArticleIdList><ArticleId IdType="pubmed">17585298</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2001 Aug 10;293(5532):1129-33</Citation><ArticleIdList><ArticleId IdType="pubmed">11498589</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2009 Jan 30;323(5914):623-6</Citation><ArticleIdList><ArticleId IdType="pubmed">19179528</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Gen Genet. 1998 Aug;259(2):216-23</Citation><ArticleIdList><ArticleId IdType="pubmed">9747713</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Biotechnol J. 2009 Aug;7(6):499-511</Citation><ArticleIdList><ArticleId IdType="pubmed">19486323</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1999 May;181(10):3277-80</Citation><ArticleIdList><ArticleId IdType="pubmed">10322033</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 2008 Apr;190(7):2629-32</Citation><ArticleIdList><ArticleId IdType="pubmed">18223080</ArticleId></ArticleIdList></Reference><Reference><Citation>BMC Evol Biol. 2007;7 Suppl 2:S4</Citation><ArticleIdList><ArticleId IdType="pubmed">17767732</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Bioinformatics. 2008;2008:420747</Citation><ArticleIdList><ArticleId IdType="pubmed">19956698</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Jun 9;281(23):15662-70</Citation><ArticleIdList><ArticleId IdType="pubmed">16595667</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1995 Sep;109(1):153-9</Citation><ArticleIdList><ArticleId IdType="pubmed">7480319</ArticleId></ArticleIdList></Reference><Reference><Citation>J Comput Chem. 2004 Oct;25(13):1605-12</Citation><ArticleIdList><ArticleId IdType="pubmed">15264254</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Proteomics. 2007 Nov;6(11):1980-96</Citation><ArticleIdList><ArticleId IdType="pubmed">17644812</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1995 Mar;107(3):719-723</Citation><ArticleIdList><ArticleId IdType="pubmed">12228396</ArticleId></ArticleIdList></Reference><Reference><Citation>Amino Acids. 2006 Mar;30(2):127-42</Citation><ArticleIdList><ArticleId IdType="pubmed">16547652</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2008 Mar;1780(3):410-20</Citation><ArticleIdList><ArticleId IdType="pubmed">17913366</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):849-59</Citation><ArticleIdList><ArticleId IdType="pubmed">15103130</ArticleId></ArticleIdList></Reference><Reference><Citation>Trends Plant Sci. 2002 May;7(5):193-5</Citation><ArticleIdList><ArticleId IdType="pubmed">11992820</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1993 Mar 15;212(3):693-704</Citation><ArticleIdList><ArticleId IdType="pubmed">8385008</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2000 Mar;122(3):907-14</Citation><ArticleIdList><ArticleId IdType="pubmed">10712555</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Genet. 1982 Jul;5(2):89-92</Citation><ArticleIdList><ArticleId IdType="pubmed">24186223</ArticleId></ArticleIdList></Reference><Reference><Citation>Bioinformatics. 2003 May 1;19(7):874-81</Citation><ArticleIdList><ArticleId IdType="pubmed">12724298</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell. 2005 Jul;17(7):2089-106</Citation><ArticleIdList><ArticleId IdType="pubmed">15923352</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Protoc Bioinformatics. 2006 Oct;Chapter 5:Unit 5.6</Citation><ArticleIdList><ArticleId IdType="pubmed">18428767</ArticleId></ArticleIdList></Reference><Reference><Citation>Brain Res. 1997 Dec 5;778(1):99-106</Citation><ArticleIdList><ArticleId IdType="pubmed">9462881</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 2006 Jul 1;34(Web Server issue):W504-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16845059</ArticleId></ArticleIdList></Reference><Reference><Citation>Microbiology. 1999 Sep;145 ( Pt 9):2221-7</Citation><ArticleIdList><ArticleId IdType="pubmed">10517575</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2008;3(4):e1994</Citation><ArticleIdList><ArticleId IdType="pubmed">18431481</ArticleId></ArticleIdList></Reference><Reference><Citation>Subcell Biochem. 2006;39:181-205</Citation><ArticleIdList><ArticleId IdType="pubmed">17121276</ArticleId></ArticleIdList></Reference><Reference><Citation>BMC Genomics. 2006;7:205</Citation><ArticleIdList><ArticleId IdType="pubmed">16901339</ArticleId></ArticleIdList></Reference><Reference><Citation>FEMS Microbiol Lett. 1997 Oct 15;155(2):223-9</Citation><ArticleIdList><ArticleId IdType="pubmed">9351205</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Microbiol. 2008 Jan;56(1):6-13</Citation><ArticleIdList><ArticleId IdType="pubmed">17851715</ArticleId></ArticleIdList></Reference><Reference><Citation>Microbiol Rev. 1996 Mar;60(1):44-69</Citation><ArticleIdList><ArticleId IdType="pubmed">8852895</ArticleId></ArticleIdList></Reference><Reference><Citation>Bioinformatics. 2001 Sep;17(9):849-50</Citation><ArticleIdList><ArticleId IdType="pubmed">11590105</ArticleId></ArticleIdList></Reference><Reference><Citation>Gene. 1989 Apr 15;77(1):51-9</Citation><ArticleIdList><ArticleId IdType="pubmed">2744487</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Microbiol. 1960 Apr;22:369-78</Citation><ArticleIdList><ArticleId IdType="pubmed">13793162</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Mol Biol. 1998 Aug;37(6):1013-22</Citation><ArticleIdList><ArticleId IdType="pubmed">9700073</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Evol. 2007 Aug;24(8):1596-9</Citation><ArticleIdList><ArticleId IdType="pubmed">17488738</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2007 Jun;144(2):890-903</Citation><ArticleIdList><ArticleId IdType="pubmed">17434988</ArticleId></ArticleIdList></Reference><Reference><Citation>Proteins. 2007 Feb 1;66(2):279-303</Citation><ArticleIdList><ArticleId IdType="pubmed">17080462</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1998 Sep;118(1):275-83</Citation><ArticleIdList><ArticleId IdType="pubmed">9733547</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1966 Dec 28;22(2):325-33</Citation><ArticleIdList><ArticleId IdType="pubmed">5339688</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Afrique du Sud</li></country></list><tree><noCountry><name sortKey="Davids, Faezah" sort="Davids, Faezah" uniqKey="Davids F" first="Faezah" last="Davids">Faezah Davids</name><name sortKey="Ingle, Robert A" sort="Ingle, Robert A" uniqKey="Ingle R" first="Robert A" last="Ingle">Robert A. Ingle</name><name sortKey="Mandala, Salvatore" sort="Mandala, Salvatore" uniqKey="Mandala S" first="Salvatore" last="Mandalà">Salvatore Mandalà</name><name sortKey="Marineo, Sandra" sort="Marineo, Sandra" uniqKey="Marineo S" first="Sandra" last="Marineo">Sandra Marineo</name><name sortKey="Sewell, Bryan T" sort="Sewell, Bryan T" uniqKey="Sewell B" first="Bryan T" last="Sewell">Bryan T. Sewell</name></noCountry><country name="Afrique du Sud"><noRegion><name sortKey="Petersen, Lindsay N" sort="Petersen, Lindsay N" uniqKey="Petersen L" first="Lindsay N" last="Petersen">Lindsay N. Petersen</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/MetalBindProtPlantV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000227 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000227 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= MetalBindProtPlantV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:20023146
|texte= The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:20023146" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a MetalBindProtPlantV1
| This area was generated with Dilib version V0.6.38. |  |