Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus.
Nat Commun
; 7: 12070, 2016 06 22.
Article
in En
| MEDLINE
| ID: mdl-27329342
ABSTRACT
Retroviral reverse transcriptase (RT) of Moloney murine leukemia virus (MoMLV) is expressed in the form of a large Gag-Pol precursor protein by suppression of translational termination in which the maximal efficiency of stop codon read-through depends on the interaction between MoMLV RT and peptidyl release factor 1 (eRF1). Here, we report the crystal structure of MoMLV RT in complex with eRF1. The MoMLV RT interacts with the C-terminal domain of eRF1 via its RNase H domain to sterically occlude the binding of peptidyl release factor 3 (eRF3) to eRF1. Promotion of read-through by MoMLV RNase H prevents nonsense-mediated mRNA decay (NMD) of mRNAs. Comparison of our structure with that of HIV RT explains why HIV RT cannot interact with eRF1. Our results provide a mechanistic view of how MoMLV manipulates the host translation termination machinery for the synthesis of its own proteins.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptide Chain Termination, Translational
/
Peptide Termination Factors
/
RNA-Directed DNA Polymerase
/
Moloney murine leukemia virus
Limits:
Animals
/
Humans
Language:
En
Journal:
Nat Commun
Journal subject:
BIOLOGIA
/
CIENCIA
Year:
2016
Document type:
Article
Affiliation country:
Singapur