TRANSLATION INITIATION AT ALTERNATE IN-FRAME AUG CODONS IN THE RABIES VIRUS PHOSPHOPROTEIN MESSENGER-RNA IS MEDIATED BY A RIBOSOMAL LEAKY SCANNING MECHANISM
TRANSLATION INITIATION AT ALTERNATE IN-FRAME AUG CODONS IN THE RABIES VIRUS PHOSPHOPROTEIN MESSENGER-RNA IS MEDIATED BY A RIBOSOMAL LEAKY SCANNING MECHANISM
复制标题
DOI:
10.1128/jvi.69.2.707-712.1995
复制
发表时间:
1995-02-01
影响因子:
5.4
通讯作者:
BLONDEL, D
中科院分区:
文献类型:
--
作者:
CHENIK, M;CHEBLI, K;BLONDEL, D
The phosphoprotein of rabies virus is a 297 amino-acid polypeptide encoded by the longest open reading frame of the P gene. Immunoprecipitation experiments using a monoclonal antiserum directed against the P protein detected the P protein and at least four additional shorter products in infected cells, cells transfected with a plasmid encoding the wild-type P protein, and purified virus (CVS strain). By means of deletion analyses, these proteins were shown to be translated from secondary downstream in-frame AUG initiation codons. Immunofluorescence experiments indicated that all these P products were found in the cytoplasm of transfected cells; however, the proteins initiated from the third, fourth, and fifth AUG codons were found mostly in the nucleus. Changes in the 5'-terminal region of the P mRNA (including site-specific mutations, deletions, and insertions) demonstrated that a leaky scanning mechanism is responsible for translation initiation of the P gene at several sites.