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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2004-1-13
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pubmed:databankReference |
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pubmed:abstractText |
Gene expression is a coordinated multistep process that begins with transcription and RNA processing in the nucleus followed by mRNA export to the cytoplasm for translation. Here we report the identification of a protein, Sus1, which functions in both transcription and mRNA export. Sus1 is a nuclear protein with a concentration at the nuclear pores. Biochemical analyses show that Sus1 interacts with SAGA, a large intranuclear histone acetylase complex involved in transcription initiation, and with the Sac3-Thp1 complex, which functions in mRNA export with specific nuclear pore proteins at the nuclear basket. DNA macroarray analysis revealed that Sus1 is required for transcription regulation. Moreover, chromatin immunoprecipitation showed that Sus1 is associated with the promoter of a SAGA-dependent gene during transcription activation. Finally, mRNA export is impaired in sus1 mutants. These data provide an unexpected connection between the SAGA histone acetylase complex and the mRNA export machinery.
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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/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleocytoplasmic Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Porins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/SAC3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thp1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/YRA1 protein, S cerevisiae
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
116
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
75-86
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:14718168-Acetyltransferases,
pubmed-meshheading:14718168-Active Transport, Cell Nucleus,
pubmed-meshheading:14718168-Amino Acid Sequence,
pubmed-meshheading:14718168-Base Sequence,
pubmed-meshheading:14718168-Cell Nucleus,
pubmed-meshheading:14718168-DNA, Complementary,
pubmed-meshheading:14718168-Fungal Proteins,
pubmed-meshheading:14718168-Gene Expression Regulation, Fungal,
pubmed-meshheading:14718168-Genes, Lethal,
pubmed-meshheading:14718168-Genes, Regulator,
pubmed-meshheading:14718168-Histone Acetyltransferases,
pubmed-meshheading:14718168-Molecular Sequence Data,
pubmed-meshheading:14718168-Nuclear Pore,
pubmed-meshheading:14718168-Nuclear Proteins,
pubmed-meshheading:14718168-Nucleocytoplasmic Transport Proteins,
pubmed-meshheading:14718168-Porins,
pubmed-meshheading:14718168-Promoter Regions, Genetic,
pubmed-meshheading:14718168-RNA, Messenger,
pubmed-meshheading:14718168-RNA-Binding Proteins,
pubmed-meshheading:14718168-Ribonucleoproteins,
pubmed-meshheading:14718168-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:14718168-Transcriptional Activation,
pubmed-meshheading:14718168-Yeasts
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pubmed:year |
2004
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pubmed:articleTitle |
Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery.
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pubmed:affiliation |
Biochemie-Zentrum der Universität Heidelberg (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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