Document Detail


La proteins from Drosophila melanogaster and Saccharomyces cerevisiae: a yeast homolog of the La autoantigen is dispensable for growth.
MedLine Citation:
PMID:  8035818     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The human autoantigen La is a 50-kDa protein which binds to the 3' termini of virtually all nascent polymerase III transcripts. Experiments with mammalian transcription extracts have led to the proposal that the La protein is required for multiple rounds of transcription by RNA polymerase III (E. Gottlieb and J. A. Steitz, EMBO J. 8:851-861, 1989; R. J. Maraia, D. J. Kenan, and J. D. Keene, Mol. Cell. Biol. 14:2147-2158, 1994). Although La protein homologs have been identified in a variety of vertebrate species, the protein has not been identified in invertebrates. In order to begin a genetic analysis of La protein function, we have characterized homologs of the La protein in the fruit fly Drosophila melanogaster and the yeast Saccharomyces cerevisiae. We show that both the Drosophila and yeast La proteins are bound to precursors of polymerase III RNAs in vivo. The Drosophila and yeast proteins resemble the human La protein in their biochemical properties, as both proteins can be partially purified from cells by a procedure previously devised to purify the human protein. Similarly to vertebrate La proteins, the Drosophila and yeast homologs preferentially bind RNAs that terminate with a 3' hydroxyl. Despite the fact that the La protein is conserved between humans and Saccharomyces cerevisiae, yeast cells containing a null allele of the gene encoding the La protein are viable, suggesting that another protein(s) plays a functionally redundant role.
Authors:
C J Yoo; S L Wolin
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular and cellular biology     Volume:  14     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  1994 Aug 
Date Detail:
Created Date:  1994-08-15     Completed Date:  1994-08-15     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5412-24     Citation Subset:  IM    
Affiliation:
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/L32988;  L33023
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Autoantigens / genetics*
Base Sequence
Chromosome Mapping
Cloning, Molecular
DNA Primers / chemistry
Drosophila melanogaster / genetics*,  physiology*
Fungal Proteins / genetics*
Genes, Fungal*
Genes, Insect*
Molecular Sequence Data
Mutagenesis, Insertional
Nuclear Proteins / genetics,  metabolism
Plant Proteins / genetics
RNA Polymerase III / metabolism
RNA, Ribosomal, 5S / metabolism
RNA-Binding Proteins / genetics*
Ribonucleoproteins / genetics*
Saccharomyces cerevisiae / physiology*
Saccharomyces cerevisiae Proteins*
Sequence Alignment
Sequence Homology, Amino Acid
Grant Support
ID/Acronym/Agency:
GM48410/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Autoantigens; 0/DNA Primers; 0/Fungal Proteins; 0/LHP1 protein, S cerevisiae; 0/Nuclear Proteins; 0/Plant Proteins; 0/RNA, Ribosomal, 5S; 0/RNA-Binding Proteins; 0/Ribonucleoproteins; 0/SS-B antigen; 0/Saccharomyces cerevisiae Proteins; EC 2.7.7.-/RNA Polymerase III
Comments/Corrections

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