DETERMINATION OF POLYPROTEIN PROCESSING SITES BY AMINO TERMINAL SEQUENCING OF NONSTRUCTURAL PROTEINS ENCODED BY PLUM POX POTYVIRUS

被引：20

作者：

MARTIN, MT ^{[1
]}

OTIN, CL ^{[1
]}

LAIN, S ^{[1
]}

GARCIA, JA ^{[1
]}

机构：

[1] UNIV OVIEDO,FAC MED,DEPT BIOL FUNC,OVIEDO,SPAIN

来源：

VIRUS RESEARCH | 1990年 / 15卷 / 02期

关键词：

D O I：

10.1016/0168-1702(90)90001-R

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Nonstructural proteins of plum pox potyvirus were partially purified following a procedure described for the isolation of tobacco etch virus nuclear inclusion proteins. Plum pox virus proteins with electrophoretic mobilities corresponding to 49, 59 and 68 kDa reacted with antibodies against the 49 kDa and 54 kDa components of the nuclear inclusions and the 70 kDa component of the cylindrical inclusions of tobacco etch virus, respectively. Further purification by size exclusion high performance liquid chromatography or SDS-polyacrylamide gel electrophoresis, and amino terminal amino acid sequencing permitted the location in the plum pox virus polyprotein of the cleavage sites from which the 49 kDa (NIa-type, protease), 59 kDa (NIb-type, putative RNA replicase), and 68 kDa (CI-type) proteins originate. A 110 kDa protein which copurified with the plum pox virus inclusion proteins reacted with both anti-NIa and anti-NIb sera and had the same amino terminus as the plum pox virus 49 kDa protein, indicating that it is a non-processed 49-59 kDa polypeptide. © 1990.

引用

页码：97 / 106

页数：10

共 33 条

[1] THE NUCLEOTIDE-SEQUENCE OF THE CODING REGION OF TOBACCO ETCH VIRUS GENOMIC RNA - EVIDENCE FOR THE SYNTHESIS OF A SINGLE POLYPROTEIN [J].