SEQUENCE COMPARISON OF 5 POLYMERASES (L-PROTEINS) OF UNSEGMENTED NEGATIVE-STRAND RNA VIRUSES - THEORETICAL ASSIGNMENT OF FUNCTIONAL DOMAINS

被引:440
作者
POCH, O
BLUMBERG, BM
BOUGUELERET, L
TORDO, N
机构
[1] INST PASTEUR, UNITE INFORMAT SCI, F-75724 PARIS 15, FRANCE
[2] INST PASTEUR, UNITE RAGE, F-75724 PARIS 15, FRANCE
[3] UNIV ROCHESTER, DEPT NEUROL, ROCHESTER, NY 14642 USA
[4] UNIV ROCHESTER, DEPT MICROBIOL, ROCHESTER, NY 14642 USA
关键词
D O I
10.1099/0022-1317-71-5-1153
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The large (L) protein subunit of unsegmented negative-strand RNA virus polymerases is thought to be responsible for the majority of enzymic activities involved in viral transcription and replication. In order to gain insight into this multifunctional role we compared the deduced amino acid sequences of five L proteins of rhabdoviruses (vesicular stomatitis virus and rabies virus) or paramyxoviruses (Sendai virus, Newcastle disease virus and measles virus). Statistical analysis showed that they share an atypical amino acid usage, outlining the uniqueness of the negative-strand virus life style. Similarity studies between L proteins traced evolutionary relationships in partial disagreement with the present taxonomic arrangement of this group of viruses. The five L proteins exhibit a high degree of homology along most of their length, with strongly invariant amino acids embedded in conserved blocks separated by variable regions, suggesting a structure of concatenated functional domains. The most highly conserved central block contains the probable active site for RNA synthesis. We tentatively identified some other functional sites, distributed around this central core, that would naturally work together to assure the polymerase activity. This provides detailed guidelines for the future study of L proteins by site-directed mutagenesis.
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页码:1153 / 1162
页数:10
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