ANALYSIS OF BIOLOGICAL FUNCTION OF POLY(ADP-RIBOSYL)ATION IN DROSOPHILA-MELANOGASTER

被引:1
作者
MIWA, M [1 ]
HANAI, S [1 ]
MASUDA, H [1 ]
KOYAMA, Y [1 ]
HAYASHI, T [1 ]
YOSHIDA, Y [1 ]
POLTRONIERI, P [1 ]
MAESHIMA, K [1 ]
KOBAYASHI, S [1 ]
OKADA, M [1 ]
UCHIDA, K [1 ]
机构
[1] UNIV TSUKUBA,INST BIOL SCI,TSUKUBA,IBARAKI 305,JAPAN
关键词
ADP-RIBOSYLATION; NAD; ZINC FINGER; LEUCINE ZIPPER;
D O I
10.1016/0300-9084(96)88162-4
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
To understand the biological function of poly(ADP-ribosyl)ation of proteins, we have isolated and characterized the gene for poly(ADP-ribose) polymerase from Drosophila melanogaster. Two approaches were taken to analyze the function of the poly(ADP-ribosyl)ation reaction. The first is analysis of the homology of the amino acid sequences of poly(ADP-ribose) polymerase from phylogenetically different eukaryotes, namely human, mouse, bovine, chicken, Xenopus laevis and Drosophila melanogaster and elucidation of the conserved amino acid sequences that appear to be important for the function of poly(ADP-ribose) polymerase. Analysis of the recombinant poly(ADP ribose) polymerase which had truncated or mutated motifs expressed in E coli would confirm the importance of the conserved amino acid sequence. The interaction of poly(ADP-ribose) polymerase with other proteins involved in DNA repair, replication, recombination and transcription will clarify the function of poly(ADP-ribosyl)ation. The second approach is to get the mutants which have disruption in the poly(ADP-ribose) polymerase gene and to analyse the phenotypes of these mutants. The characterization of these mutants will be discussed.
引用
收藏
页码:466 / 471
页数:6
相关论文
共 32 条
[1]   CLONING AND EXPRESSION OF CDNA FOR HUMAN POLY(ADP-RIBOSE) POLYMERASE [J].
ALKHATIB, HM ;
CHEN, D ;
CHERNEY, B ;
BHATIA, K ;
NOTARIO, V ;
GIRI, C ;
STEIN, G ;
SLATTERY, E ;
ROEDER, RG ;
SMULSON, ME .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (05) :1224-1228
[2]  
ALTHAUS FR, 1987, ADP RIBOSYLATION PRO, P1
[3]  
BENJAMIN RC, 1980, J BIOL CHEM, V255, P493
[4]  
BOULIKAS T, 1992, ANTICANCER RES, V12, P885
[5]   CDNA SEQUENCE, PROTEIN-STRUCTURE, AND CHROMOSOMAL LOCATION OF THE HUMAN-GENE FOR POLY(ADP-RIBOSE) POLYMERASE [J].
CHERNEY, BW ;
MCBRIDE, OW ;
CHEN, D ;
ALKHATIB, H ;
BHATIA, K ;
HENSLEY, P ;
SMULSON, ME .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (23) :8370-8374
[6]   POLY(ADP-RIBOSE) POLYMERASE - A MOLECULAR NICK-SENSOR [J].
DEMURCIA, G ;
DEMURCIA, JM .
TRENDS IN BIOCHEMICAL SCIENCES, 1994, 19 (04) :172-176
[7]   THE 2ND ZINC-FINGER DOMAIN OF POLY(ADP-RIBOSE) POLYMERASE DETERMINES SPECIFICITY FOR SINGLE-STRANDED BREAKS IN DNA [J].
GRADWOHL, G ;
DEMURCIA, JM ;
MOLINETE, M ;
SIMONIN, F ;
KOKEN, M ;
HOEIJMAKERS, JHJ ;
DEMURCIA, G .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1990, 87 (08) :2990-2994
[8]   SEQUENCE AND ORGANIZATION OF THE MOUSE POLY (ADP-RIBOSE) POLYMERASE GENE [J].
HUPPI, K ;
BHATIA, K ;
SIWARSKI, D ;
KLINMAN, D ;
CHERNEY, B ;
SMULSON, M .
NUCLEIC ACIDS RESEARCH, 1989, 17 (09) :3387-3401
[9]  
IKEJIMA M, 1990, J BIOL CHEM, V265, P21907
[10]   CHICKEN POLY(ADP-RIBOSE) SYNTHETASE - COMPLETE DEDUCED AMINO-ACID-SEQUENCE AND COMPARISON WITH MAMMALIAN ENZYME SEQUENCES [J].
ITTEL, ME ;
GARNIER, JM ;
JELTSCH, JM ;
NIEDERGANG, CP .
GENE, 1991, 102 (02) :157-164