Source:http://linkedlifedata.com/resource/pubmed/id/17400406
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2007-5-7
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pubmed:abstractText |
HTL1, a small gene of Saccharomyces cerevisiae, encodes a 78-aminoacid peptide that influences the performance of a wide range of cellular processes [Lanzuolo, C., Ederle, S., Pollice, A., Russo, F., Storlazzi, A., Pulitzer, J.F., 2001. The HTL1 gene,YCR020W-b of Saccharomyces cerevisiae is necessary for growth at 37 degrees C, and for the conservation of chromosome stability and fertility. Yeast, 18, 1317-1330]. Genetic interactions and co-immunoprecipitation experiments indicate a role for Htl1p in functions controlled by RSC, a multiprotein, ATP-dependent, chromatin-remodeling complex [Lu, Y.M., Lin, Y.R., Tsai, A., Hsao, Y.S., Li, C.C., Cheng, M.Y., 2003. Dissecting the pet18 mutation in Saccharomyces cerevisiae: HTL1 encodes a 7-kDa polypeptide that interacts with components of the RSC complex. Mol. Genet. Genomics., 269, 321-330] [Romeo, M.J., Angus-Hill, M.L., Sobering, A.K., Kamada, Y., Cairns, B.R., Levin, D.E., 2002. HTL1 encodes a novel factor that interacts with the Rsc chromatin-remodeling complex in Saccharomyces cerevisiae. Mol. Cell. Biol., 22, 8165-8174]. Htl1p and RSC components, share the property of associating with TBP a component of general multiprotein transcription factor TFIID [Sanders, S.L., Jennings, J., Canutescu, A., Link, A.J., Weil, P.A., 2002. Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry. Mol. Cell. Biol. 22, 4723-4738]. We confirm, by integrating genetic and biochemical experiments, that Htl1p binding to the RSC complex is direct and physiologically relevant and show that it is mediated by Rsc8p, a core component of the RSC complex. Deletion of HTL1, like depletion of RSC core subunits [Moreira, J.M., Holmberg, S., 1999. Transcriptional repression of the yeast CHA1 gene requires the chromatin-remodeling complex Rsc. Embo J., 18, 2836-2844], leads to constitutive transcription of the CHA1 locus. This transcriptional phenotype exhibits variable penetrance. Deletion of HTL1 also leads to hydroxyurea hypersensitivity at 30 degrees C, suggesting a defect in replication/repair. This defect leads, during cell growth, to selection of mutations at the SIR3 locus that suppress hydroxyurea sensitivity.
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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/DNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Formamides,
http://linkedlifedata.com/resource/pubmed/chemical/HTL1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyurea,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RSC complex, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SIR3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Silent Information Regulator...,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/formamide
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0378-1119
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
395
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
72-85
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pubmed:dateRevised |
2009-7-23
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pubmed:meshHeading |
pubmed-meshheading:17400406-Amino Acid Sequence,
pubmed-meshheading:17400406-Base Sequence,
pubmed-meshheading:17400406-Chromatin Assembly and Disassembly,
pubmed-meshheading:17400406-DNA, Fungal,
pubmed-meshheading:17400406-DNA-Binding Proteins,
pubmed-meshheading:17400406-Drug Resistance, Fungal,
pubmed-meshheading:17400406-Escherichia coli,
pubmed-meshheading:17400406-Formamides,
pubmed-meshheading:17400406-Genes, Fungal,
pubmed-meshheading:17400406-Hydroxyurea,
pubmed-meshheading:17400406-Molecular Sequence Data,
pubmed-meshheading:17400406-Mutation,
pubmed-meshheading:17400406-Nuclear Proteins,
pubmed-meshheading:17400406-Plasmids,
pubmed-meshheading:17400406-Recombinant Proteins,
pubmed-meshheading:17400406-Saccharomyces cerevisiae,
pubmed-meshheading:17400406-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:17400406-Sequence Homology, Amino Acid,
pubmed-meshheading:17400406-Silent Information Regulator Proteins, Saccharomyces...,
pubmed-meshheading:17400406-Transcription Factors
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pubmed:year |
2007
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pubmed:articleTitle |
A study of biochemical and functional interactions of Htl1p, a putative component of the Saccharomyces cerevisiae, Rsc chromatin-remodeling complex.
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pubmed:affiliation |
Università degli Studi di Napoli Federico II, Dipartimento di Biologia, Via Cinthia-80126-Naples, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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