|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
1998-3-24
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
RPM2 is a Saccharomyces cerevisiae nuclear gene required for normal cell growth yet the only known function of Rpm2p is as a protein subunit of yeast mitochondrial RNase P, an enzyme responsible for the 5' maturation of mitochondrial tRNAs. Since mitochondrial protein synthesis in S. cerevisiae is not essential for viability, RPM2 must provide another function in addition to its known role as a mitochondrial tRNA processing enzyme. During a search for RPM2 homologues from Kluyveromyces lactis, we recovered a K. lactis gene that compensates for the essential function but not the RNase P function of RPM2. We have named this gene SEF1 (Suppressor of the Essential Function), DNA sequence analysis of SEF1 reveals it contains a Zn(2)-Cys(6) binuclear cluster motif found in a growing number of yeast transcription factors. The SEF1 homologue of S. cerevisiae also compensates for the essential function of RPM2. The two proteins share 49% identity and 72% amino acid sequence similarity.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Catalytic,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, mitochondrial,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease P,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
0749-503X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
14
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
77-87
|
|
pubmed:dateRevised |
2005-11-17
|
|
pubmed:meshHeading |
pubmed-meshheading:9483797-Amino Acid Sequence,
pubmed-meshheading:9483797-Cloning, Molecular,
pubmed-meshheading:9483797-Endoribonucleases,
pubmed-meshheading:9483797-Fungal Proteins,
pubmed-meshheading:9483797-Genes, Fungal,
pubmed-meshheading:9483797-Genetic Complementation Test,
pubmed-meshheading:9483797-Kluyveromyces,
pubmed-meshheading:9483797-Mitochondria,
pubmed-meshheading:9483797-Molecular Sequence Data,
pubmed-meshheading:9483797-RNA,
pubmed-meshheading:9483797-RNA, Catalytic,
pubmed-meshheading:9483797-RNA, Fungal,
pubmed-meshheading:9483797-RNA, Transfer,
pubmed-meshheading:9483797-Ribonuclease P,
pubmed-meshheading:9483797-Saccharomyces cerevisiae,
pubmed-meshheading:9483797-Sequence Analysis, DNA,
pubmed-meshheading:9483797-Suppression, Genetic,
pubmed-meshheading:9483797-Transcription Factors,
pubmed-meshheading:9483797-Transformation, Genetic
|
|
pubmed:year |
1998
|
|
pubmed:articleTitle |
Kluyveromyces lactis SEF1 and its Saccharomyces cerevisiae homologue bypass the unknown essential function, but not the mitochondrial RNase P function, of the S. cerevisiae RPM2 gene.
|
|
pubmed:affiliation |
Department of Biochemistry, University of Louisville School of Medicine, KY 40292, USA.
|
|
pubmed:publicationType |
Journal Article
|
