PoplarV1, Main, Exploration, bibRecord, 001C02

Phosphorylation is an on/off switch for 5-hydroxyconiferaldehyde O-methyltransferase activity in poplar monolignol biosynthesis.

Identifieur interne : 001C02 ( Main/Exploration ); précédent : 001C01; suivant : 001C03

Phosphorylation is an on/off switch for 5-hydroxyconiferaldehyde O-methyltransferase activity in poplar monolignol biosynthesis.

Auteurs : Jack P. Wang [États-Unis] ; Ling Chuang [États-Unis] ; Philip L. Loziuk [États-Unis] ; Hao Chen [États-Unis] ; Ying-Chung Lin [États-Unis] ; Rui Shi [États-Unis] ; Guan-Zheng Qu [République populaire de Chine] ; David C. Muddiman [États-Unis] ; Ronald R. Sederoff [États-Unis] ; Vincent L. Chiang [États-Unis]

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2015.

RBID : pubmed:26109572

Descripteurs français

English descriptors

KwdEn :
- Acrolein (analogs & derivatives), Acrolein (metabolism), Amino Acid Sequence (MeSH), Binding Sites (genetics), Biocatalysis (MeSH), Catechols (metabolism), Chromatography, Liquid (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Green Fluorescent Proteins (genetics), Green Fluorescent Proteins (metabolism), Isoenzymes (genetics), Isoenzymes (metabolism), Lignin (biosynthesis), Methyltransferases (genetics), Methyltransferases (metabolism), Microscopy, Confocal (MeSH), Molecular Sequence Data (MeSH), Mutation (MeSH), Phosphoproteins (metabolism), Phosphorylation (MeSH), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (enzymology), Populus (genetics), Populus (metabolism), Proteomics (methods), Protoplasts (enzymology), Protoplasts (metabolism), Sequence Homology, Amino Acid (MeSH), Tandem Mass Spectrometry (MeSH).
MESH :
- chemical , analogs & derivatives : Acrolein.
- chemical , biosynthesis : Lignin.
- chemical , genetics : Green Fluorescent Proteins, Isoenzymes, Methyltransferases, Plant Proteins.
- chemical , metabolism : Acrolein, Catechols, Green Fluorescent Proteins, Isoenzymes, Methyltransferases, Phosphoproteins, Plant Proteins.
- enzymology : Populus, Protoplasts.
- genetics : Binding Sites, Populus.
- metabolism : Populus, Protoplasts.
- methods : Proteomics.
- Amino Acid Sequence, Biocatalysis, Chromatography, Liquid, Electrophoresis, Polyacrylamide Gel, Microscopy, Confocal, Molecular Sequence Data, Mutation, Phosphorylation, Sequence Homology, Amino Acid, Tandem Mass Spectrometry.

Abstract

Although phosphorylation has long been known to be an important regulatory modification of proteins, no unequivocal evidence has been presented to show functional control by phosphorylation for the plant monolignol biosynthetic pathway. Here, we present the discovery of phosphorylation-mediated on/off regulation of enzyme activity for 5-hydroxyconiferaldehyde O-methyltransferase 2 (PtrAldOMT2), an enzyme central to monolignol biosynthesis for lignification in stem-differentiating xylem (SDX) of Populus trichocarpa. Phosphorylation turned off the PtrAldOMT2 activity, as demonstrated in vitro by using purified phosphorylated and unphosphorylated recombinant PtrAldOMT2. Protein extracts of P. trichocarpa SDX, which contains endogenous kinases, also phosphorylated recombinant PtrAldOMT2 and turned off the recombinant protein activity. Similarly, ATP/Mn(2+)-activated phosphorylation of SDX protein extracts reduced the endogenous SDX PtrAldOMT2 activity by ∼ 60%, and dephosphorylation fully restored the activity. Global shotgun proteomic analysis of phosphopeptide-enriched P. trichocarpa SDX protein fractions identified PtrAldOMT2 monophosphorylation at Ser(123) or Ser(125) in vivo. Phosphorylation-site mutagenesis verified the PtrAldOMT2 phosphorylation at Ser(123) or Ser(125) and confirmed the functional importance of these phosphorylation sites for O-methyltransferase activity. The PtrAldOMT2 Ser(123) phosphorylation site is conserved across 93% of AldOMTs from 46 diverse plant species, and 98% of the AldOMTs have either Ser(123) or Ser(125). PtrAldOMT2 is a homodimeric cytosolic enzyme expressed more abundantly in syringyl lignin-rich fiber cells than in guaiacyl lignin-rich vessel cells. The reversible phosphorylation of PtrAldOMT2 is likely to have an important role in regulating syringyl monolignol biosynthesis of P. trichocarpa.

DOI: 10.1073/pnas.1510473112
PubMed: 26109572
PubMed Central: PMC4500226

Affiliations:

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Le document en format XML

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<term>Acrolein (metabolism)</term>
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<term>Binding Sites (genetics)</term>
<term>Biocatalysis (MeSH)</term>
<term>Catechols (metabolism)</term>
<term>Chromatography, Liquid (MeSH)</term>
<term>Electrophoresis, Polyacrylamide Gel (MeSH)</term>
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<term>Green Fluorescent Proteins (metabolism)</term>
<term>Isoenzymes (genetics)</term>
<term>Isoenzymes (metabolism)</term>
<term>Lignin (biosynthesis)</term>
<term>Methyltransferases (genetics)</term>
<term>Methyltransferases (metabolism)</term>
<term>Microscopy, Confocal (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Phosphoproteins (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Populus (enzymology)</term>
<term>Populus (genetics)</term>
<term>Populus (metabolism)</term>
<term>Proteomics (methods)</term>
<term>Protoplasts (enzymology)</term>
<term>Protoplasts (metabolism)</term>
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<term>Tandem Mass Spectrometry (MeSH)</term>
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<term>Chromatographie en phase liquide (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
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<term>Isoenzymes (métabolisme)</term>
<term>Lignine (biosynthèse)</term>
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<term>Methyltransferases (métabolisme)</term>
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<term>Mutation (MeSH)</term>
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<term>Sites de fixation (génétique)</term>
<term>Spectrométrie de masse en tandem (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Électrophorèse sur gel de polyacrylamide (MeSH)</term>
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<term>Protéines à fluorescence verte</term>
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<term>Catéchols</term>
<term>Isoenzymes</term>
<term>Methyltransferases</term>
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<term>Populus</term>
<term>Protoplastes</term>
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<term>Biocatalysis</term>
<term>Chromatography, Liquid</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Microscopy, Confocal</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
<term>Phosphorylation</term>
<term>Sequence Homology, Amino Acid</term>
<term>Tandem Mass Spectrometry</term>
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<term>Mutation</term>
<term>Phosphorylation</term>
<term>Similitude de séquences d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Although phosphorylation has long been known to be an important regulatory modification of proteins, no unequivocal evidence has been presented to show functional control by phosphorylation for the plant monolignol biosynthetic pathway. Here, we present the discovery of phosphorylation-mediated on/off regulation of enzyme activity for 5-hydroxyconiferaldehyde O-methyltransferase 2 (PtrAldOMT2), an enzyme central to monolignol biosynthesis for lignification in stem-differentiating xylem (SDX) of Populus trichocarpa. Phosphorylation turned off the PtrAldOMT2 activity, as demonstrated in vitro by using purified phosphorylated and unphosphorylated recombinant PtrAldOMT2. Protein extracts of P. trichocarpa SDX, which contains endogenous kinases, also phosphorylated recombinant PtrAldOMT2 and turned off the recombinant protein activity. Similarly, ATP/Mn(2+)-activated phosphorylation of SDX protein extracts reduced the endogenous SDX PtrAldOMT2 activity by ∼ 60%, and dephosphorylation fully restored the activity. Global shotgun proteomic analysis of phosphopeptide-enriched P. trichocarpa SDX protein fractions identified PtrAldOMT2 monophosphorylation at Ser(123) or Ser(125) in vivo. Phosphorylation-site mutagenesis verified the PtrAldOMT2 phosphorylation at Ser(123) or Ser(125) and confirmed the functional importance of these phosphorylation sites for O-methyltransferase activity. The PtrAldOMT2 Ser(123) phosphorylation site is conserved across 93% of AldOMTs from 46 diverse plant species, and 98% of the AldOMTs have either Ser(123) or Ser(125). PtrAldOMT2 is a homodimeric cytosolic enzyme expressed more abundantly in syringyl lignin-rich fiber cells than in guaiacyl lignin-rich vessel cells. The reversible phosphorylation of PtrAldOMT2 is likely to have an important role in regulating syringyl monolignol biosynthesis of P. trichocarpa.</div>
</front>
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<DateCompleted><Year>2015</Year>
<Month>10</Month>
<Day>26</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>01</Month>
<Day>09</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>112</Volume>
<Issue>27</Issue>
<PubDate><Year>2015</Year>
<Month>Jul</Month>
<Day>07</Day>
</PubDate>
</JournalIssue>
<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
<ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation>
</Journal>
<ArticleTitle>Phosphorylation is an on/off switch for 5-hydroxyconiferaldehyde O-methyltransferase activity in poplar monolignol biosynthesis.</ArticleTitle>
<Pagination><MedlinePgn>8481-6</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1510473112</ELocationID>
<Abstract><AbstractText>Although phosphorylation has long been known to be an important regulatory modification of proteins, no unequivocal evidence has been presented to show functional control by phosphorylation for the plant monolignol biosynthetic pathway. Here, we present the discovery of phosphorylation-mediated on/off regulation of enzyme activity for 5-hydroxyconiferaldehyde O-methyltransferase 2 (PtrAldOMT2), an enzyme central to monolignol biosynthesis for lignification in stem-differentiating xylem (SDX) of Populus trichocarpa. Phosphorylation turned off the PtrAldOMT2 activity, as demonstrated in vitro by using purified phosphorylated and unphosphorylated recombinant PtrAldOMT2. Protein extracts of P. trichocarpa SDX, which contains endogenous kinases, also phosphorylated recombinant PtrAldOMT2 and turned off the recombinant protein activity. Similarly, ATP/Mn(2+)-activated phosphorylation of SDX protein extracts reduced the endogenous SDX PtrAldOMT2 activity by ∼ 60%, and dephosphorylation fully restored the activity. Global shotgun proteomic analysis of phosphopeptide-enriched P. trichocarpa SDX protein fractions identified PtrAldOMT2 monophosphorylation at Ser(123) or Ser(125) in vivo. Phosphorylation-site mutagenesis verified the PtrAldOMT2 phosphorylation at Ser(123) or Ser(125) and confirmed the functional importance of these phosphorylation sites for O-methyltransferase activity. The PtrAldOMT2 Ser(123) phosphorylation site is conserved across 93% of AldOMTs from 46 diverse plant species, and 98% of the AldOMTs have either Ser(123) or Ser(125). PtrAldOMT2 is a homodimeric cytosolic enzyme expressed more abundantly in syringyl lignin-rich fiber cells than in guaiacyl lignin-rich vessel cells. The reversible phosphorylation of PtrAldOMT2 is likely to have an important role in regulating syringyl monolignol biosynthesis of P. trichocarpa.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Jack P</ForeName>
<Initials>JP</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Tree Genetics and Breeding, Northeast Forestry University, Harbin 150040, China; Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695;</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Chuang</LastName>
<ForeName>Ling</ForeName>
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</AffiliationInfo>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Hao</ForeName>
<Initials>H</Initials>
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</AffiliationInfo>
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</AffiliationInfo>
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<ForeName>Rui</ForeName>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Qu</LastName>
<ForeName>Guan-Zheng</ForeName>
<Initials>GZ</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Tree Genetics and Breeding, Northeast Forestry University, Harbin 150040, China;</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Muddiman</LastName>
<ForeName>David C</ForeName>
<Initials>DC</Initials>
<AffiliationInfo><Affiliation>W. M. Keck FT-ICR MS Laboratory for Human Health Research, Department of Chemistry, North Carolina State University, Raleigh, NC 27695.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sederoff</LastName>
<ForeName>Ronald R</ForeName>
<Initials>RR</Initials>
<AffiliationInfo><Affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695; vchiang@ncsu.edu ron_sederoff@ncsu.edu.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chiang</LastName>
<ForeName>Vincent L</ForeName>
<Initials>VL</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Tree Genetics and Breeding, Northeast Forestry University, Harbin 150040, China; Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695; vchiang@ncsu.edu ron_sederoff@ncsu.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
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<ArticleDate DateType="Electronic"><Year>2015</Year>
<Month>06</Month>
<Day>24</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Proc Natl Acad Sci U S A</MedlineTA>
<NlmUniqueID>7505876</NlmUniqueID>
<ISSNLinking>0027-8424</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C405696">5-hydroxyconiferyl aldehyde</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D002396">Catechols</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010750">Phosphoproteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C434469">syringyl monolignol</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>147336-22-9</RegistryNumber>
<NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>7864XYD3JJ</RegistryNumber>
<NameOfSubstance UI="D000171">Acrolein</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>9005-53-2</RegistryNumber>
<NameOfSubstance UI="D008031">Lignin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber>
<NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance>
</Chemical>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000171" MajorTopicYN="N">Acrolein</DescriptorName>
<QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
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<MeshHeading><DescriptorName UI="D055162" MajorTopicYN="N">Biocatalysis</DescriptorName>
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<MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018613" MajorTopicYN="N">Microscopy, Confocal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010750" MajorTopicYN="N">Phosphoproteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D040901" MajorTopicYN="N">Proteomics</DescriptorName>
<QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011523" MajorTopicYN="N">Protoplasts</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053719" MajorTopicYN="N">Tandem Mass Spectrometry</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">AldOMT</Keyword>
<Keyword MajorTopicYN="N">COMT</Keyword>
<Keyword MajorTopicYN="N">lignin</Keyword>
<Keyword MajorTopicYN="N">phosphoproteomics</Keyword>
<Keyword MajorTopicYN="N">phosphoregulation</Keyword>
</KeywordList>
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Phosphorylation is an on/off switch for 5-hydroxyconiferaldehyde O-methyltransferase activity in poplar monolignol biosynthesis.

Phosphorylation is an on/off switch for 5-hydroxyconiferaldehyde O-methyltransferase activity in poplar monolignol biosynthesis.

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