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PMID: 8654585 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Porcine polypyrimidine tract-binding protein stimulates translation initiation at the internal ribosome entry site of foot-and-mouth-disease virus.

FEBS letters ·Vol. 388 ·No. 1 ·1996-06-10 ·Pages 39-42

Niepmann M

Abstract

The cDNA for porcine polypyrimidine tract-binding protein (sPTB) was cloned. The sPTB amino acid sequence is highly homologous to the human PTB sequence (97% identity), and the sPTB sequence corresponds to that of the longest human PTB, PTB4. The specificity of binding in the UV-crosslink of sPTB to the internal ribosome entry site (IRES) of foot-and-mouth-disease virus (FMDV) is similar to that of human PTB. Purified recombinant sPTB efficiently stimulates internal translation initiation directed by the FMDV IRES in a rabbit reticulocyte lysate translation system from which the internal PTB had been depleted.

MeSH Terms
Amino Acid Sequence Animals Aphthovirus/genetics Base Sequence Binding Sites Cloning, Molecular Cross-Linking Reagents DNA-Binding Proteins/genetics,pharmacology,physiology Humans Molecular Sequence Data Peptide Chain Initiation, Translational/drug effects,physiology Polypyrimidine Tract-Binding Protein RNA, Viral/metabolism RNA-Binding Proteins/genetics,pharmacology,physiology Recombinant Fusion Proteins/biosynthesis Regulatory Sequences, Nucleic Acid/physiology Ribosomes Sequence Analysis, DNA Sequence Homology, Amino Acid Swine Ultraviolet Rays
Chemicals
Cross-Linking Reagents DNA-Binding Proteins RNA, Viral RNA-Binding Proteins Recombinant Fusion Proteins Polypyrimidine Tract-Binding Protein
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Niepmann M
Institut für Biochemie, Giessen, Germany.
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1996-06-10
Pages
39-42
Language
English
Region
England
NLM ID
0155157
Subset
IM
Databases
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