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PMID: 8483932 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 9 ·1993-05-01 ·Pages 4181-5

Baron C, Heider J, Böck A

Abstract

The SELB protein from Escherichia coli is a specialized elongation factor required for the UGA-directed insertion of the amino acid selenocysteine into selenopolypeptides. Discrimination of the UGA codon requires the presence of a recognition element within the mRNA, which is located at the 3' side of the UGA codon; a hairpin structure can be formed within this mRNA region. By gel shift assays, a specific interaction between SELB and the mRNA recognition element could be demonstrated. Footprinting experiments, using nucleases or iodine as cleaving agents, showed that SELB binds to the loop region of the hairpin structure. In the presence of selenocysteinyl-tRNA, SELB formed a complex with the charged tRNA and the mRNA. The results indicate that targeted insertion of selenocysteine is accomplished by the binding of the SELB protein to this mRNA recognition element, resulting in the formation of a selenocysteinyl-tRNA.SELB complex at the mRNA in the immediate neighborhood of the UGA codon.

Related Genes
fdhF
MeSH Terms
Bacterial Proteins/isolation & purification,metabolism Base Sequence Escherichia coli/genetics,metabolism Formate Dehydrogenases/genetics Genes, Bacterial Hydrogenase/genetics Models, Genetic Molecular Sequence Data Multienzyme Complexes/genetics Nucleic Acid Conformation Peptide Elongation Factors/isolation & purification,metabolism Protein Binding Protein Biosynthesis Proteins/genetics RNA, Messenger/genetics,isolation & purification,metabolism RNA, Transfer, Amino Acyl/metabolism Selenoproteins Substrate Specificity Transcription, Genetic
Chemicals
Bacterial Proteins Multienzyme Complexes Peptide Elongation Factors Proteins RNA, Messenger RNA, Transfer, Amino Acyl SelB protein, Bacteria Selenoproteins selenocysteinyl-tRNA Hydrogenase Formate Dehydrogenases formate hydrogenlyase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Baron C
Lehrstuhl für Mikrobiologie, Universität München, Germany.
Heider J
Böck A
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.9.4181
Published
1993-05-01
Pages
4181-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC46470
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.90.9.4181 PMC Full Text View journal details
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