共 20 条
MEASLES-VIRUS PHOSPHOPROTEIN (P) REQUIRES THE NH2-TERMINAL AND COOH-TERMINAL DOMAINS FOR INTERACTIONS WITH THE NUCLEOPROTEIN (N) BUT ONLY THE COOH TERMINUS FOR INTERACTIONS WITH ITSELF
被引:77
作者:

HARTY, RN
论文数: 0 引用数: 0
h-index: 0
机构:
MT SINAI SCH MED,DEPT MICROBIOL,NEW YORK,NY 10029 MT SINAI SCH MED,DEPT MICROBIOL,NEW YORK,NY 10029

PALESE, P
论文数: 0 引用数: 0
h-index: 0
机构:
MT SINAI SCH MED,DEPT MICROBIOL,NEW YORK,NY 10029 MT SINAI SCH MED,DEPT MICROBIOL,NEW YORK,NY 10029
机构:
[1] MT SINAI SCH MED,DEPT MICROBIOL,NEW YORK,NY 10029
关键词:
D O I:
10.1099/0022-1317-76-11-2863
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:
A mammalian two-hybrid system was used to characterize protein-protein interactions between the measles virus nucleoprotein (N) and phosphoprotein (P). Progressive deletions at both the amino- and carboxy-termini of P facilitated the mapping of two distinct domains on P that are important for interaction with N: (i) a domain mapping predominantly within the C-terminal 100 amino acids and (ii) a domain composed of the extreme amino-terminal residues. Using the same two-hybrid assay, we discovered that the P protein interacts strongly with itself. In contrast to the N-P interaction, only a single C-proximal domain of P was essential for P-P interaction.
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页码:2863 / 2867
页数:5
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