Comparative sequence analysis of ribonucleases HII, III, II PH and D

被引:163
作者
Mian, IS [1 ]
机构
[1] UNIV CALIF SANTA CRUZ, SINSHEIMER LABS, SANTA CRUZ, CA 95064 USA
关键词
D O I
10.1093/nar/25.16.3187
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
Escherichia coli ribonucleases (RNases) HII, III, II, PH and D have been used to characterise new and known viral, bacterial, archaeal and eucaryotic sequences similar to these endo- (Hit and III) and exoribonucleases (It, PH and D), Statistical models, hidden Markov models (HMMs), were created for the RNase HII, III, II, PH and D families as well as a double-stranded RNA binding domain present in RNase III, Results suggest that the RNase D family, which includes Werner syndrome protein and the 100 kDa antigenic component of the human polymyositis scleroderma (PMSCL) autoantigen, is a 3'-->5' exoribonuclease structurally and functionally related to the 3'-->5' exodeoxyribonuclease domain of DNA polymerases, Polynucleotide phosphorylases and the RNase PH family, which includes the 75 kDa PMSCL autoantigen, possess a common domain suggesting similar structures and mechanisms of action for these 3'-->5' phosphorolytic enzymes, Examination of HMM-generated multiple sequence alignments for each family suggest amino acids that may be important for their structure, substrate binding and/or catalysis.
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页码:3187 / 3195
页数:9
相关论文
共 64 条
[1]   RNase III cleaves eukaryotic preribosomal RNA at a U3 snoRNP-dependent site [J].
AbouElela, S ;
Igel, H ;
Ares, M .
CELL, 1996, 85 (01) :115-124
[2]   AMINO-ACID SUBSTITUTION MATRICES FROM AN INFORMATION THEORETIC PERSPECTIVE [J].
ALTSCHUL, SF .
JOURNAL OF MOLECULAR BIOLOGY, 1991, 219 (03) :555-565
[3]  
ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1006/jmbi.1990.9999
[4]   RNA PROCESSING IN PROKARYOTIC CELLS [J].
APIRION, D ;
MICZAK, A .
BIOESSAYS, 1993, 15 (02) :113-120
[5]   HIDDEN MARKOV-MODELS OF BIOLOGICAL PRIMARY SEQUENCE INFORMATION [J].
BALDI, P ;
CHAUVIN, Y ;
HUNKAPILLER, T ;
MCCLURE, MA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (03) :1059-1063
[6]  
Barrett C, 1997, COMPUT APPL BIOSCI, V13, P191
[7]   ALSCRIPT - A TOOL TO FORMAT MULTIPLE SEQUENCE ALIGNMENTS [J].
BARTON, GJ .
PROTEIN ENGINEERING, 1993, 6 (01) :37-40
[8]   STRUCTURAL BASIS FOR THE 3'-5' EXONUCLEASE ACTIVITY OF ESCHERICHIA-COLI DNA-POLYMERASE-I - A 2 METAL-ION MECHANISM [J].
BEESE, LS ;
STEITZ, TA .
EMBO JOURNAL, 1991, 10 (01) :25-33
[9]   STRUCTURE OF DNA-POLYMERASE-I KLENOW FRAGMENT BOUND TO DUPLEX DNA [J].
BEESE, LS ;
DERBYSHIRE, V ;
STEITZ, TA .
SCIENCE, 1993, 260 (5106) :352-355
[10]   A CONSERVED 3'-]5' EXONUCLEASE ACTIVE-SITE IN PROKARYOTIC AND EUKARYOTIC DNA-POLYMERASES [J].
BERNAD, A ;
BLANCO, L ;
LAZARO, JM ;
MARTIN, G ;
SALAS, M .
CELL, 1989, 59 (01) :219-228