Distinctive Nuclear Localization Signals in the Oomycete Phytophthora sojae.
Identifieur interne : 000A25 ( Main/Exploration ); précédent : 000A24; suivant : 000A26Distinctive Nuclear Localization Signals in the Oomycete Phytophthora sojae.
Auteurs : Yufeng Fang [États-Unis] ; Hyo Sang Jang [États-Unis] ; Gregory W. Watson [États-Unis] ; Dulani P. Wellappili [États-Unis] ; Brett M. Tyler [États-Unis]Source :
- Frontiers in microbiology [ 1664-302X ] ; 2017.
Abstract
To date, nuclear localization signals (NLSs) that target proteins to nuclei in oomycetes have not been defined, but have been assumed to be the same as in higher eukaryotes. Here, we use the soybean pathogen Phytophthora sojae as a model to investigate these sequences in oomycetes. By establishing a reliable in vivo NLS assay based on confocal microscopy, we found that many canonical monopartite and bipartite classical NLSs (cNLSs) mediated nuclear import poorly in P. sojae. We found that efficient localization of P. sojae nuclear proteins by cNLSs requires additional basic amino acids at distal sites or collaboration with other NLSs. We found that several representatives of another well-characterized NLS, proline-tyrosine NLS (PY-NLS) also functioned poorly in P. sojae. To characterize PY-NLSs in P. sojae, we experimentally defined the residues required by functional PY-NLSs in three P. sojae nuclear-localized proteins. These results showed that functional P. sojae PY-NLSs include an additional cluster of basic residues for efficient nuclear import. Finally, analysis of several highly conserved P. sojae nuclear proteins including ribosomal proteins and core histones revealed that these proteins exhibit a similar but stronger set of sequence requirements for nuclear targeting compared with their orthologs in mammals or yeast.
DOI: 10.3389/fmicb.2017.00010
PubMed: 28210240
PubMed Central: PMC5288373
Affiliations:
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Watson</name><affiliation wicri:level="2"><nlm:affiliation>Molecular and Cellular Biology Program, Oregon State UniversityCorvallis, OR, USA; Biological and Population Health Sciences, Oregon State UniversityCorvallis, OR, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Molecular and Cellular Biology Program, Oregon State UniversityCorvallis, OR, USA; Biological and Population Health Sciences, Oregon State UniversityCorvallis, OR</wicri:regionArea><placeName><region type="state">Oregon</region></placeName></affiliation></author><author><name sortKey="Wellappili, Dulani P" sort="Wellappili, Dulani P" uniqKey="Wellappili D" first="Dulani P" last="Wellappili">Dulani P. 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Tyler</name><affiliation wicri:level="2"><nlm:affiliation>Interdisciplinary Ph.D. Program in Genetics, Bioinformatics and Computational Biology, Virginia TechBlacksburg, VA, USA; Center for Genome Research and Biocomputing and Department of Botany and Plant Pathology, Oregon State UniversityCorvallis, OR, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Interdisciplinary Ph.D. Program in Genetics, Bioinformatics and Computational Biology, Virginia TechBlacksburg, VA, USA; Center for Genome Research and Biocomputing and Department of Botany and Plant Pathology, Oregon State UniversityCorvallis, OR</wicri:regionArea><placeName><region type="state">Oregon</region></placeName></affiliation></author></analytic><series><title level="j">Frontiers in microbiology</title><idno type="ISSN">1664-302X</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To date, nuclear localization signals (NLSs) that target proteins to nuclei in oomycetes have not been defined, but have been assumed to be the same as in higher eukaryotes. Here, we use the soybean pathogen <i>Phytophthora sojae</i> as a model to investigate these sequences in oomycetes. By establishing a reliable <i>in vivo</i> NLS assay based on confocal microscopy, we found that many canonical monopartite and bipartite classical NLSs (cNLSs) mediated nuclear import poorly in <i>P. sojae</i>. We found that efficient localization of <i>P. sojae</i> nuclear proteins by cNLSs requires additional basic amino acids at distal sites or collaboration with other NLSs. We found that several representatives of another well-characterized NLS, proline-tyrosine NLS (PY-NLS) also functioned poorly in <i>P. sojae</i>. To characterize PY-NLSs in <i>P. sojae</i>, we experimentally defined the residues required by functional PY-NLSs in three <i>P. sojae</i> nuclear-localized proteins. These results showed that functional <i>P. sojae</i> PY-NLSs include an additional cluster of basic residues for efficient nuclear import. Finally, analysis of several highly conserved <i>P. sojae</i> nuclear proteins including ribosomal proteins and core histones revealed that these proteins exhibit a similar but stronger set of sequence requirements for nuclear targeting compared with their orthologs in mammals or yeast.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">28210240</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1664-302X</ISSN><JournalIssue CitedMedium="Print"><Volume>8</Volume><PubDate><Year>2017</Year></PubDate></JournalIssue><Title>Frontiers in microbiology</Title><ISOAbbreviation>Front Microbiol</ISOAbbreviation></Journal><ArticleTitle>Distinctive Nuclear Localization Signals in the Oomycete <i>Phytophthora sojae</i>.</ArticleTitle><Pagination><MedlinePgn>10</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fmicb.2017.00010</ELocationID><Abstract><AbstractText>To date, nuclear localization signals (NLSs) that target proteins to nuclei in oomycetes have not been defined, but have been assumed to be the same as in higher eukaryotes. Here, we use the soybean pathogen <i>Phytophthora sojae</i> as a model to investigate these sequences in oomycetes. By establishing a reliable <i>in vivo</i> NLS assay based on confocal microscopy, we found that many canonical monopartite and bipartite classical NLSs (cNLSs) mediated nuclear import poorly in <i>P. sojae</i>. We found that efficient localization of <i>P. sojae</i> nuclear proteins by cNLSs requires additional basic amino acids at distal sites or collaboration with other NLSs. We found that several representatives of another well-characterized NLS, proline-tyrosine NLS (PY-NLS) also functioned poorly in <i>P. sojae</i>. To characterize PY-NLSs in <i>P. sojae</i>, we experimentally defined the residues required by functional PY-NLSs in three <i>P. sojae</i> nuclear-localized proteins. These results showed that functional <i>P. sojae</i> PY-NLSs include an additional cluster of basic residues for efficient nuclear import. Finally, analysis of several highly conserved <i>P. sojae</i> nuclear proteins including ribosomal proteins and core histones revealed that these proteins exhibit a similar but stronger set of sequence requirements for nuclear targeting compared with their orthologs in mammals or yeast.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fang</LastName><ForeName>Yufeng</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Interdisciplinary Ph.D. Program in Genetics, Bioinformatics and Computational Biology, Virginia TechBlacksburg, VA, USA; Center for Genome Research and Biocomputing and Department of Botany and Plant Pathology, Oregon State UniversityCorvallis, OR, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jang</LastName><ForeName>Hyo Sang</ForeName><Initials>HS</Initials><AffiliationInfo><Affiliation>Department of Environmental and Molecular Toxicology, Oregon State University Corvallis, OR, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Watson</LastName><ForeName>Gregory W</ForeName><Initials>GW</Initials><AffiliationInfo><Affiliation>Molecular and Cellular Biology Program, Oregon State UniversityCorvallis, OR, USA; Biological and Population Health Sciences, Oregon State UniversityCorvallis, OR, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wellappili</LastName><ForeName>Dulani P</ForeName><Initials>DP</Initials><AffiliationInfo><Affiliation>Center for Genome Research and Biocomputing and Department of Botany and Plant Pathology, Oregon State University Corvallis, OR, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tyler</LastName><ForeName>Brett M</ForeName><Initials>BM</Initials><AffiliationInfo><Affiliation>Interdisciplinary Ph.D. Program in Genetics, Bioinformatics and Computational Biology, Virginia TechBlacksburg, VA, USA; Center for Genome Research and Biocomputing and Department of 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