File Download
 
Links for fulltext
(May Require Subscription)
 
Supplementary

Article: OsNOA1/RIF1 is a functional homolog of AtNOA1/RIF1: Implication for a highly conserved plant cGTPase essential for chloroplast function
  • Basic View
  • Metadata View
  • XML View
TitleOsNOA1/RIF1 is a functional homolog of AtNOA1/RIF1: Implication for a highly conserved plant cGTPase essential for chloroplast function
 
AuthorsLiu, H1 3
Lau, E2
Lam, MPY2
Chu, H3
Li, S1
Huang, G1
Guo, P1
Wang, J4
Jiang, L4
Chu, IK2
Lo, C3
Tao, Y1
 
KeywordsChloroplast translation
NOA1/RIF1
Os02g01440
Plant cGTPase
Rice (Oryza sativa)
 
Issue Date2010
 
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NPH
 
CitationNew Phytologist, 2010, v. 187 n. 1, p. 83-105 [How to Cite?]
DOI: http://dx.doi.org/10.1111/j.1469-8137.2010.03264.x
 
AbstractSummary: •The bacterial protein YqeH is a circularly permuted GTPase with homologs encoded by plant nuclear genomes. The rice homolog OsNOA1/RIF1 is encoded by the single-copy gene Os02g01440. OsNOA1/RIF1 is expressed in different tissues and is light-inducible. The OsNOA1/RIF1-EYFP fusion protein was targeted to chloroplasts in transgenic Arabidopsis plants. In addition, the rice homolog was able to rescue most of the growth phenotypes in an Arabidopsis rif1 mutant.•Rice (Oryza sativa) OsNOA1/RIF1 RNAi mutant seedlings were chlorotic with reduced pigment contents and lower photosystem II (PSII) efficiency. However, the expressions of the chloroplast-encoded genes rbcL, atpB, psaA and psbA were not affected. By contrast, reduced abundance of the chloroplast 16S rRNA was observed in the mutant.•Quantitative iTRAQ-LC-MS/MS proteomics investigations revealed proteome changes in the rice mutant consistent with the expected functional role of OsNOA1/RIF1 in chloroplast translation. The RNAi mutant showed significantly decreased expression levels of chloroplast-encoded proteins as well as nuclear-encoded components of chloroplast enzyme complexes. Conversely, upregulation of some classes of nonchloroplastic proteins, such as glycolytic and phenylpropanoid pathway enzymes, was detected.•Our work provides independent indications that a highly conserved nuclear-encoded cGTPase of likely prokaryotic origin is essential for proper chloroplast ribosome assembly and/or translation in plants. © The Authors (2010). Journal compilation © New Phytologist Trust (2010).
 
ISSN0028-646X
2012 Impact Factor: 6.736
2012 SCImago Journal Rankings: 2.650
 
DOIhttp://dx.doi.org/10.1111/j.1469-8137.2010.03264.x
 
ISI Accession Number IDWOS:000278395100011
Funding AgencyGrant Number
National High Technology Research and Development Program of China2006AA10A102
Research Grants Council of Hong KongHKU7527/06M
HKU200811159080
Funding Information:

This work was supported by the National High Technology Research and Development Program of China (2006AA10A102) to Yuezhi Tao as well as the Research Grants Council of Hong Kong (HKU7527/06M) and HKU Seed Funding Programme (200811159080) to Clive Lo. We are grateful to Professor Jirong Huang (National Key Laboratory of Plant Molecular Genetics, Shanghai Institute for Biological Sciences) for his helpful discussions on our investigations. We also thank Dr P. Leon (Instituto de Biotechnologia-UNAM) for providing the DXS antibodies.

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLiu, H
 
dc.contributor.authorLau, E
 
dc.contributor.authorLam, MPY
 
dc.contributor.authorChu, H
 
dc.contributor.authorLi, S
 
dc.contributor.authorHuang, G
 
dc.contributor.authorGuo, P
 
dc.contributor.authorWang, J
 
dc.contributor.authorJiang, L
 
dc.contributor.authorChu, IK
 
dc.contributor.authorLo, C
 
dc.contributor.authorTao, Y
 
dc.date.accessioned2011-07-27T01:26:19Z
 
dc.date.available2011-07-27T01:26:19Z
 
dc.date.issued2010
 
dc.description.abstractSummary: •The bacterial protein YqeH is a circularly permuted GTPase with homologs encoded by plant nuclear genomes. The rice homolog OsNOA1/RIF1 is encoded by the single-copy gene Os02g01440. OsNOA1/RIF1 is expressed in different tissues and is light-inducible. The OsNOA1/RIF1-EYFP fusion protein was targeted to chloroplasts in transgenic Arabidopsis plants. In addition, the rice homolog was able to rescue most of the growth phenotypes in an Arabidopsis rif1 mutant.•Rice (Oryza sativa) OsNOA1/RIF1 RNAi mutant seedlings were chlorotic with reduced pigment contents and lower photosystem II (PSII) efficiency. However, the expressions of the chloroplast-encoded genes rbcL, atpB, psaA and psbA were not affected. By contrast, reduced abundance of the chloroplast 16S rRNA was observed in the mutant.•Quantitative iTRAQ-LC-MS/MS proteomics investigations revealed proteome changes in the rice mutant consistent with the expected functional role of OsNOA1/RIF1 in chloroplast translation. The RNAi mutant showed significantly decreased expression levels of chloroplast-encoded proteins as well as nuclear-encoded components of chloroplast enzyme complexes. Conversely, upregulation of some classes of nonchloroplastic proteins, such as glycolytic and phenylpropanoid pathway enzymes, was detected.•Our work provides independent indications that a highly conserved nuclear-encoded cGTPase of likely prokaryotic origin is essential for proper chloroplast ribosome assembly and/or translation in plants. © The Authors (2010). Journal compilation © New Phytologist Trust (2010).
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationNew Phytologist, 2010, v. 187 n. 1, p. 83-105 [How to Cite?]
DOI: http://dx.doi.org/10.1111/j.1469-8137.2010.03264.x
 
dc.identifier.doihttp://dx.doi.org/10.1111/j.1469-8137.2010.03264.x
 
dc.identifier.eissn1469-8137
 
dc.identifier.epage105
 
dc.identifier.hkuros170887
 
dc.identifier.isiWOS:000278395100011
Funding AgencyGrant Number
National High Technology Research and Development Program of China2006AA10A102
Research Grants Council of Hong KongHKU7527/06M
HKU200811159080
Funding Information:

This work was supported by the National High Technology Research and Development Program of China (2006AA10A102) to Yuezhi Tao as well as the Research Grants Council of Hong Kong (HKU7527/06M) and HKU Seed Funding Programme (200811159080) to Clive Lo. We are grateful to Professor Jirong Huang (National Key Laboratory of Plant Molecular Genetics, Shanghai Institute for Biological Sciences) for his helpful discussions on our investigations. We also thank Dr P. Leon (Instituto de Biotechnologia-UNAM) for providing the DXS antibodies.

 
dc.identifier.issn0028-646X
2012 Impact Factor: 6.736
2012 SCImago Journal Rankings: 2.650
 
dc.identifier.issue1
 
dc.identifier.pmid20456051
 
dc.identifier.scopuseid_2-s2.0-77954588661
 
dc.identifier.spage83
 
dc.identifier.urihttp://hdl.handle.net/10722/135031
 
dc.identifier.volume187
 
dc.languageeng
 
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NPH
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofNew Phytologist
 
dc.relation.referencesReferences in Scopus
 
dc.rightsThe definitive version is available at www.blackwell-synergy.com
 
dc.subject.meshArabidopsis - enzymology
 
dc.subject.meshChloroplasts - enzymology
 
dc.subject.meshConserved Sequence - genetics
 
dc.subject.meshNitric Oxide Synthase - chemistry
 
dc.subject.meshPlant Proteins - chemistry - genetics - metabolism
 
dc.subjectChloroplast translation
 
dc.subjectNOA1/RIF1
 
dc.subjectOs02g01440
 
dc.subjectPlant cGTPase
 
dc.subjectRice (Oryza sativa)
 
dc.titleOsNOA1/RIF1 is a functional homolog of AtNOA1/RIF1: Implication for a highly conserved plant cGTPase essential for chloroplast function
 
dc.typeArticle
 
<?xml encoding="utf-8" version="1.0"?>
<item><contributor.author>Liu, H</contributor.author>
<contributor.author>Lau, E</contributor.author>
<contributor.author>Lam, MPY</contributor.author>
<contributor.author>Chu, H</contributor.author>
<contributor.author>Li, S</contributor.author>
<contributor.author>Huang, G</contributor.author>
<contributor.author>Guo, P</contributor.author>
<contributor.author>Wang, J</contributor.author>
<contributor.author>Jiang, L</contributor.author>
<contributor.author>Chu, IK</contributor.author>
<contributor.author>Lo, C</contributor.author>
<contributor.author>Tao, Y</contributor.author>
<date.accessioned>2011-07-27T01:26:19Z</date.accessioned>
<date.available>2011-07-27T01:26:19Z</date.available>
<date.issued>2010</date.issued>
<identifier.citation>New Phytologist, 2010, v. 187 n. 1, p. 83-105</identifier.citation>
<identifier.issn>0028-646X</identifier.issn>
<identifier.uri>http://hdl.handle.net/10722/135031</identifier.uri>
<description.abstract>Summary: &#8226;The bacterial protein YqeH is a circularly permuted GTPase with homologs encoded by plant nuclear genomes. The rice homolog OsNOA1/RIF1 is encoded by the single-copy gene Os02g01440. OsNOA1/RIF1 is expressed in different tissues and is light-inducible. The OsNOA1/RIF1-EYFP fusion protein was targeted to chloroplasts in transgenic Arabidopsis plants. In addition, the rice homolog was able to rescue most of the growth phenotypes in an Arabidopsis rif1 mutant.&#8226;Rice (Oryza sativa) OsNOA1/RIF1 RNAi mutant seedlings were chlorotic with reduced pigment contents and lower photosystem II (PSII) efficiency. However, the expressions of the chloroplast-encoded genes rbcL, atpB, psaA and psbA were not affected. By contrast, reduced abundance of the chloroplast 16S rRNA was observed in the mutant.&#8226;Quantitative iTRAQ-LC-MS/MS proteomics investigations revealed proteome changes in the rice mutant consistent with the expected functional role of OsNOA1/RIF1 in chloroplast translation. The RNAi mutant showed significantly decreased expression levels of chloroplast-encoded proteins as well as nuclear-encoded components of chloroplast enzyme complexes. Conversely, upregulation of some classes of nonchloroplastic proteins, such as glycolytic and phenylpropanoid pathway enzymes, was detected.&#8226;Our work provides independent indications that a highly conserved nuclear-encoded cGTPase of likely prokaryotic origin is essential for proper chloroplast ribosome assembly and/or translation in plants. &#169; The Authors (2010). Journal compilation &#169; New Phytologist Trust (2010).</description.abstract>
<language>eng</language>
<publisher>Blackwell Publishing Ltd. The Journal&apos;s web site is located at http://www.blackwellpublishing.com/journals/NPH</publisher>
<relation.ispartof>New Phytologist</relation.ispartof>
<rights>The definitive version is available at www.blackwell-synergy.com</rights>
<subject>Chloroplast translation</subject>
<subject>NOA1/RIF1</subject>
<subject>Os02g01440</subject>
<subject>Plant cGTPase</subject>
<subject>Rice (Oryza sativa)</subject>
<subject.mesh>Arabidopsis - enzymology</subject.mesh>
<subject.mesh>Chloroplasts - enzymology</subject.mesh>
<subject.mesh>Conserved Sequence - genetics</subject.mesh>
<subject.mesh>Nitric Oxide Synthase - chemistry</subject.mesh>
<subject.mesh>Plant Proteins - chemistry - genetics - metabolism</subject.mesh>
<title>OsNOA1/RIF1 is a functional homolog of AtNOA1/RIF1: Implication for a highly conserved plant cGTPase essential for chloroplast function</title>
<type>Article</type>
<description.nature>link_to_OA_fulltext</description.nature>
<identifier.doi>10.1111/j.1469-8137.2010.03264.x</identifier.doi>
<identifier.pmid>20456051</identifier.pmid>
<identifier.scopus>eid_2-s2.0-77954588661</identifier.scopus>
<identifier.hkuros>170887</identifier.hkuros>
<relation.references>http://www.scopus.com/mlt/select.url?eid=2-s2.0-77954588661&amp;selection=ref&amp;src=s&amp;origin=recordpage</relation.references>
<identifier.volume>187</identifier.volume>
<identifier.issue>1</identifier.issue>
<identifier.spage>83</identifier.spage>
<identifier.epage>105</identifier.epage>
<identifier.eissn>1469-8137</identifier.eissn>
<identifier.isi>WOS:000278395100011</identifier.isi>
<publisher.place>United Kingdom</publisher.place>
<bitstream.url>http://hub.hku.hk/bitstream/10722/135031/1/re01.htm</bitstream.url>
</item>
Author Affiliations
  1. Zhejiang Academy of Agricultural Sciences
  2. The University of Hong Kong
  3. School of Biological Sciences
  4. Chinese University of Hong Kong