ANTIGENIC PROTEIN-SPECIFIC FOR C3H STRAIN MOUSE IS A MITOCHONDRIAL STRESS-70 PROTEIN

被引:20
作者
MICHIKAWA, Y
BABA, T
ARAI, Y
SAKAKURA, T
TANAKA, M
KUSAKABE, M
机构
[1] INST PHYS & CHEM RES RIKEN,CELL BIOL LAB,TSUKUBA,IBARAKI 305,JAPAN
[2] UNIV TSUKUBA,INST APPL BIOCHEM,TSUKUBA,IBARAKI 305,JAPAN
[3] NAGOYA UNIV,FAC MED,DEPT BIOMED CHEM,NAGOYA,AICHI 466,JAPAN
关键词
D O I
10.1006/bbrc.1993.2238
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cells derived from C3H strain mouse produce an antigenic protein (CSA) specifci for this strain [Kusakabe, M., et al. (1988) J. Cell Biol. 107, 257-265]. To examine the molecular basis of CSA, cDNA cloning of the antigenic protein was carried out. The deduced amino acid sequence demonstrates that CSA is the same protein as peptide-binding protein74 (PBP74), a novel member of the stress-70 family. However, comparison of the PBP74/CSA sequences between C3H/HeN and BALB/c strain mice reveals the substitution of two amino acids in the substrate-recognition domain of the stress-70 protein. Western blot analysis indicates that one out of these two residues, arginine at residue 578 in the PBP74/CSA sequence of C3H mouse, contributes to the immunogenicity of CSA. Moreover, the subcellular localization of PBP74/CSA in mitochondria is also demonstrated by immunohistochemical analysis using anti-CSA monoclonal antibody. Thus, it is interesting that a genetic marker sequence in mice is located on the gene encoding a mitochondrial stress-70 protein. © 1993 Academic Press, Inc.
引用
收藏
页码:223 / 232
页数:10
相关论文
共 28 条
[1]   MAJOR HEAT-SHOCK GENE OF DROSOPHILA AND THE ESCHERICHIA-COLI HEAT-INDUCIBLE DNAK GENE ARE HOMOLOGOUS [J].
BARDWELL, JCA ;
CRAIG, EA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (03) :848-852
[2]   SCREENING GAMMAGT RECOMBINANT CLONES BY HYBRIDIZATION TO SINGLE PLAQUES INSITU [J].
BENTON, WD ;
DAVIS, RW .
SCIENCE, 1977, 196 (4286) :180-182
[3]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[4]   ISOLATION OF BIOLOGICALLY-ACTIVE RIBONUCLEIC-ACID FROM SOURCES ENRICHED IN RIBONUCLEASE [J].
CHIRGWIN, JM ;
PRZYBYLA, AE ;
MACDONALD, RJ ;
RUTTER, WJ .
BIOCHEMISTRY, 1979, 18 (24) :5294-5299
[5]  
Chou P Y, 1978, Adv Enzymol Relat Areas Mol Biol, V47, P45
[6]   SSC1, AN ESSENTIAL MEMBER OF THE YEAST HSP70 MULTIGENE FAMILY, ENCODES A MITOCHONDRIAL PROTEIN [J].
CRAIG, EA ;
KRAMER, J ;
SHILLING, J ;
WERNERWASHBURNE, M ;
HOLMES, S ;
KOSICSMITHERS, J ;
NICOLET, CM .
MOLECULAR AND CELLULAR BIOLOGY, 1989, 9 (07) :3000-3008
[7]   A CASE FOR CHAPERONES IN ANTIGEN PROCESSING [J].
DENAGEL, DC ;
PIERCE, SK .
IMMUNOLOGY TODAY, 1992, 13 (03) :86-89
[8]   CLONING OF THE GENE ENCODING PEPTIDE-BINDING PROTEIN-74 SHOWS THAT IT IS A NEW MEMBER OF THE HEAT-SHOCK PROTEIN-70 FAMILY [J].
DOMANICO, SZ ;
DENAGEL, DC ;
DAHLSEID, JN ;
GREEN, JM ;
PIERCE, SK .
MOLECULAR AND CELLULAR BIOLOGY, 1993, 13 (06) :3598-3610
[9]   A TECHNIQUE FOR RADIOLABELING DNA RESTRICTION ENDONUCLEASE FRAGMENTS TO HIGH SPECIFIC ACTIVITY [J].
FEINBERG, AP ;
VOGELSTEIN, B .
ANALYTICAL BIOCHEMISTRY, 1983, 132 (01) :6-13
[10]   PROTEIN FOLDING IN THE CELL [J].
GETHING, MJ ;
SAMBROOK, J .
NATURE, 1992, 355 (6355) :33-45