p23 and HSP20/α-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families

被引:118
作者
Garcia-Ranea, JA
Mirey, G
Camonis, J
Valencia, A [1 ]
机构
[1] Ctr Nacl Biotecnol, Prot Design Grp, Madrid 28049, Spain
[2] Inst Curie, INSERM, U528, F-75248 Paris 05, France
来源
FEBS LETTERS | 2002年 / 529卷 / 2-3期
关键词
p23; co-chaperone; sHSP20; chaperone; NudC; Sgt1; B5+B5R flavo-hemo cytochrome NAD(P)H; oxidoreductase type B; Rar1; conserved protein domain;
D O I
10.1016/S0014-5793(02)03321-5
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
We identified families of proteins characterized by the presence of a domain similar to human p23 protein, which include proteins such as Sgt1, involved in the yeast kinetochore assembly; melusin, involved in specific interactions with the cytoplasmic integrin beta1 domain; Rar1, related to pathogenic resistance in plants, and to development in animals; B5+B5R flavo-hemo cytochrome NAD(P)H oxidoreductase type B in humans and mice; and NudC, involved in nucleus migration during mitosis. We also found that p23 and the HSP20/alpha-crystallin family of heat shock proteins, which share the same three-dimensional folding, show a pattern of conserved residues that points to a common origin in the evolution of both protein domains. The p23 and HSP20/a-crystallin phylogenetic relationship and their similar role in chaperone activity suggest a common function, probably involving protein-protein interaction, for those proteins containing p23-like domains. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:162 / 167
页数:6
相关论文
共 66 条
[31]   AMINO-ACID-SEQUENCE OF YEAST HEMOGLOBIN - A 2-DOMAIN STRUCTURE [J].
IWAASA, H ;
TAKAGI, T ;
SHIKAMA, K .
JOURNAL OF MOLECULAR BIOLOGY, 1992, 227 (03) :948-954
[32]   CHARACTERIZATION OF A NOVEL 23-KILODALTON PROTEIN OF UNACTIVE PROGESTERONE-RECEPTOR COMPLEXES [J].
JOHNSON, JL ;
BEITO, TG ;
KRCO, CJ ;
TOFT, DO .
MOLECULAR AND CELLULAR BIOLOGY, 1994, 14 (03) :1956-1963
[33]   Protein folding in vivo: Unraveling complex pathways [J].
Johnson, JL ;
Craig, EA .
CELL, 1997, 90 (02) :201-204
[34]   Aggresomes: A cellular response to misfolded proteins [J].
Johnston, JA ;
Ward, CL ;
Kopito, RR .
JOURNAL OF CELL BIOLOGY, 1998, 143 (07) :1883-1898
[35]   Hidden Markov models for detecting remote protein homologies [J].
Karplus, K ;
Barrett, C ;
Hughey, R .
BIOINFORMATICS, 1998, 14 (10) :846-856
[36]   Crystal structure of a small heat-shock protein [J].
Kim, KK ;
Kim, R ;
Kim, SH .
NATURE, 1998, 394 (6693) :595-599
[37]   Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by αB-crystallin [J].
Koyama, Y ;
Goldman, JE .
AMERICAN JOURNAL OF PATHOLOGY, 1999, 154 (05) :1563-1572
[38]   HIDDEN MARKOV-MODELS IN COMPUTATIONAL BIOLOGY - APPLICATIONS TO PROTEIN MODELING [J].
KROGH, A ;
BROWN, M ;
MIAN, IS ;
SJOLANDER, K ;
HAUSSLER, D .
JOURNAL OF MOLECULAR BIOLOGY, 1994, 235 (05) :1501-1531
[39]   CYTOCHROME B(5)-FOLD - AN ADAPTABLE MODULE [J].
LEDERER, F .
BIOCHIMIE, 1994, 76 (07) :674-692
[40]   Siah-1, SIP, and Ebi collaborate in a novel pathway for β-catenin degradation linked to p53 responses [J].
Matsuzawa, S ;
Reed, JC .
MOLECULAR CELL, 2001, 7 (05) :915-926