THE GAG-POL ENCODED PROTEINASE OF AN AVIAN RETROVIRUS EXPRESSED IN ESCHERICHIA-COLI CAN PRODUCE A NOVEL PROTEINASE (PR+IIEGLY) THAT IS 2 AMINO-ACIDS LARGER AT ITS CARBOXY-TERMINAL REGION THAN THE MAJOR GAG PROTEINASE (PR)

被引:1
作者
BRYNDA, J [1 ]
FABRY, M [1 ]
HOREJSI, M [1 ]
SEDLACEK, J [1 ]
机构
[1] ACAD SCI CZECH REPUBL, INST MOLEC GENET, DEPT GENE MANIPULAT, CR-16637 PRAGUE 6, CZECH REPUBLIC
关键词
D O I
10.1006/viro.1995.1065
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Gag-Pol frameshift translational products of avian retroviruses (e.g., myeloblastosis associated virus, MAV) contain a putative proteinase species of 131 amino acids that maps between the NC/PR and the PR/RT processing sites. Expression in Escherichia coli of an in-frame PR precursor that contains the natural NC/PR processing site and is translationally terminated at the PR/RT site leads to formation of a Gag-Pol proteinase of the expected molecular size (131 amino acids) and a novel PR product of 126 amino acids. This product extends 2 amino acids downstream of the gag-encoded 124 amino acids, and its proteolytic cleavage is promoted by conditions favorable for enzyme catalysis, is blocked by a specific MAV proteinase inhibitor, and can be demonstrated also for corresponding peptide substrates. The new self-processing cleavage product is termed PR(+IleGly) and exhibits similar, but slower, catalytic parameters than those of the Gag PR. (C) 1995 Academic Press, Inc.
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页码:185 / 190
页数:6
相关论文
共 23 条
[1]  
ANDREANSKY M, 1991, FEBS LETT, V87, P129
[2]   AMINO-ACIDS ENCODED DOWNSTREAM OF GAG ARE NOT REQUIRED BY ROUS-SARCOMA VIRUS PROTEASE DURING GAG-MEDIATED ASSEMBLY [J].
BENNETT, RP ;
RHEE, S ;
CRAVEN, RC ;
HUNTER, E ;
WILLS, JW .
JOURNAL OF VIROLOGY, 1991, 65 (01) :272-280
[3]  
BIZUB D, 1991, J BIOL CHEM, V266, P4951
[4]   HUMAN IMMUNODEFICIENCY VIRUS PROTEASE EXPRESSED IN ESCHERICHIA-COLI EXHIBITS AUTOPROCESSING AND SPECIFIC MATURATION OF THE GAG PRECURSOR [J].
DEBOUCK, C ;
GORNIAK, JG ;
STRICKLER, JE ;
MEEK, TD ;
METCALF, BW ;
ROSENBERG, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (24) :8903-8906
[5]   EXPRESSION OF VIRUS-ENCODED PROTEINASES - FUNCTIONAL AND STRUCTURAL SIMILARITIES WITH CELLULAR ENZYMES [J].
DOUGHERTY, WG ;
SEMLER, BL .
MICROBIOLOGICAL REVIEWS, 1993, 57 (04) :781-822
[6]   AN 11-KDA FORM OF HUMAN IMMUNODEFICIENCY VIRUS PROTEASE EXPRESSED IN ESCHERICHIA-COLI IS SUFFICIENT FOR ENZYMATIC-ACTIVITY [J].
GRAVES, MC ;
LIM, JJ ;
HEIMER, EP ;
KRAMER, RA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1988, 85 (08) :2449-2453
[7]  
GRINDE B, 1992, J BIOL CHEM, V267, P9481
[8]   EXPRESSION OF THE ROUS-SARCOMA VIRUS POL GENE BY RIBOSOMAL FRAMESHIFTING [J].
JACKS, T ;
VARMUS, HE .
SCIENCE, 1985, 230 (4731) :1237-1242
[9]   SIGNALS FOR RIBOSOMAL FRAMESHIFTING IN THE ROUS-SARCOMA VIRUS GAG-POL REGION [J].
JACKS, T ;
MADHANI, HD ;
MASIARZ, FR ;
VARMUS, HE .
CELL, 1988, 55 (03) :447-458
[10]   STRUCTURE OF THE ASPARTIC PROTEASE FROM ROUS-SARCOMA RETROVIRUS REFINED AT 2-A RESOLUTION [J].
JASKOLSKI, M ;
MILLER, M ;
RAO, JKM ;
LEIS, J ;
WLODAWER, A .
BIOCHEMISTRY, 1990, 29 (25) :5889-5898