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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
50
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pubmed:dateCreated |
2001-12-12
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pubmed:abstractText |
Saccharomyces cerevisiae Ste24p is a multispanning membrane protein implicated in the CAAX proteolysis step that occurs during biogenesis of the prenylated a-factor mating pheromone. Whether Ste24p acts directly as a CAAX protease or indirectly to activate a downstream protease has not yet been established. In this study, we demonstrate that purified, detergent-solubilized Ste24p directly mediates CAAX proteolysis in a zinc-dependent manner. We also show that Ste24p mediates a separate proteolytic step, the first NH(2)-terminal cleavage in a-factor maturation. These results establish that Ste24p functions both as a bona fide COOH-terminal CAAX protease and as an a-factor NH(2)-terminal protease. Importantly, this study is the first to directly demonstrate that a eukaryotic multispanning membrane protein can possess intrinsic proteolytic activity.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase K,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proprotein Convertases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/RCE1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/STE24 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc,
http://linkedlifedata.com/resource/pubmed/chemical/mating factor
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
46798-806
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11581258-Amino Acid Sequence,
pubmed-meshheading:11581258-Catalysis,
pubmed-meshheading:11581258-Detergents,
pubmed-meshheading:11581258-Dose-Response Relationship, Drug,
pubmed-meshheading:11581258-Endopeptidase K,
pubmed-meshheading:11581258-Endopeptidases,
pubmed-meshheading:11581258-Genotype,
pubmed-meshheading:11581258-Mass Spectrometry,
pubmed-meshheading:11581258-Membrane Proteins,
pubmed-meshheading:11581258-Metalloendopeptidases,
pubmed-meshheading:11581258-Methylation,
pubmed-meshheading:11581258-Models, Biological,
pubmed-meshheading:11581258-Molecular Sequence Data,
pubmed-meshheading:11581258-Peptides,
pubmed-meshheading:11581258-Plasmids,
pubmed-meshheading:11581258-Proprotein Convertases,
pubmed-meshheading:11581258-Protein Binding,
pubmed-meshheading:11581258-Protein Precursors,
pubmed-meshheading:11581258-Protein Prenylation,
pubmed-meshheading:11581258-Protein Structure, Tertiary,
pubmed-meshheading:11581258-Saccharomyces cerevisiae,
pubmed-meshheading:11581258-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11581258-Sequence Homology, Amino Acid,
pubmed-meshheading:11581258-Zinc
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pubmed:year |
2001
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pubmed:articleTitle |
The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor.
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pubmed:affiliation |
Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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