Source:http://linkedlifedata.com/resource/pubmed/id/17714429
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2007-10-9
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pubmed:abstractText |
The Arabidopsis E3 ligase AtCHIP was found to interact with FtsH1, a subunit of the chloroplast FtsH protease complex. FtsH1 can be ubiquitylated by AtCHIP in vitro, and the steady-state level of FtsH1 is reduced in AtCHIP-over-expressing plants under high-intensity light conditions, suggesting that the ubiquitylation of FtsH1 by AtCHIP might lead to the degradation of FtsH1 in vivo. Furthermore, the steady-state level of another subunit of the chloroplast FtsH protease complex, FtsH2, is also reduced in AtCHIP-over-expressing plants under high-intensity light conditions, and FtsH2 interacts physically with AtCHIP in vivo, suggesting the possibility that FtsH2 is also a substrate protein for AtCHIP in plant cells. A substrate of FtsH protease in vivo, the photosystem II reaction center protein D1, is not efficiently removed by FtsH in AtCHIP-over-expressing plants under high-intensity light conditions, supporting the assumption that FtsH subunits are substrates of AtCHIP in vivo, and that AtCHIP over-expression may lead to a reduced level of FtsH in chloroplasts. AtCHIP interacts with cytosolic Hsp70 and the precursors of FtsH1 and FtsH2 in the cytoplasm, and Hsp70 also interacts with FtsH1, and these protein-protein interactions appear to be increased under high-intensity light conditions, suggesting that Hsp70 might be partly responsible for the increased degradation of the substrates of Hsp70, such as FtsH1 and FtsH2, in AtCHIP-over-expressing plants under high-intensity light conditions. Therefore, AtCHIP, together with Hsp70, may play an important role in protein quality control in chloroplasts.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CHIP protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloproteases,
http://linkedlifedata.com/resource/pubmed/chemical/Photosystem II Protein Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0960-7412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
52
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
309-21
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pubmed:meshHeading |
pubmed-meshheading:17714429-Arabidopsis,
pubmed-meshheading:17714429-Arabidopsis Proteins,
pubmed-meshheading:17714429-Cell Death,
pubmed-meshheading:17714429-Chloroplasts,
pubmed-meshheading:17714429-Cytosol,
pubmed-meshheading:17714429-Gene Expression Regulation, Plant,
pubmed-meshheading:17714429-HSP70 Heat-Shock Proteins,
pubmed-meshheading:17714429-Light,
pubmed-meshheading:17714429-Metalloproteases,
pubmed-meshheading:17714429-Photosystem II Protein Complex,
pubmed-meshheading:17714429-Plant Leaves,
pubmed-meshheading:17714429-Protein Processing, Post-Translational,
pubmed-meshheading:17714429-Two-Hybrid System Techniques,
pubmed-meshheading:17714429-Ubiquitin-Protein Ligases,
pubmed-meshheading:17714429-Ubiquitination
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pubmed:year |
2007
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pubmed:articleTitle |
The E3 ligase AtCHIP ubiquitylates FtsH1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts.
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pubmed:affiliation |
Department of Biological Sciences, Texas Tech University, Lubbock, TX 79409, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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