The insertion of palindromic repeats in the evolution of proteins

被引:40
作者
Claverie, JM [1 ]
Ogata, H [1 ]
机构
[1] CNRS, UMR 1889, AVENTIS, Inst Biol Struct & Microbiol,IFR 88, FR-13402 Marseille, France
关键词
D O I
10.1016/S0968-0004(02)00036-1
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
The current theory of protein evolution is that all contemporary proteins are derived from an ancestral subset. However, each new sequenced genome exhibits many genes with no detectable homologues in other species, leading to the paradoxical picture of a universal ancestor with more genes than any of its progeny. Standard explanations indicate that fast evolving genes might disappear into the 'twilight zone' of sequence similarity. Regardless of the size of the original ancestral subset, its origin and the potential mechanisms of its subsequent enlargement are rarely addressed. Sequencing of Rickettsia conorii genome recently led to the discovery of three families of repeat-mobile elements frequently inserted into the middle of protein coding genes. Although not yet identified in other species of bacteria, this discovery has provided the first clear evidence for the de novo creation of long protein segments (up to 50 amino acid residues) by repeat insertion. Based on previous results and theories on the coding potential of palindromic elements, we speculate that their insertion and mobility might have played a significant role in the early stages of protein evolution.
引用
收藏
页码:75 / 80
页数:6
相关论文
共 42 条
[1]  
[Anonymous], [No title captured]
[2]   The InterPro database, an integrated documentation resource for protein families, domains and functional sites [J].
Apweiler, R ;
Attwood, TK ;
Bairoch, A ;
Bateman, A ;
Birney, E ;
Biswas, M ;
Bucher, P ;
Cerutti, T ;
Corpet, F ;
Croning, MDR ;
Durbin, R ;
Falquet, L ;
Fleischmann, W ;
Gouzy, J ;
Hermjakob, H ;
Hulo, N ;
Jonassen, I ;
Kahn, D ;
Kanapin, A ;
Karavidopoulou, Y ;
Lopez, R ;
Marx, B ;
Mulder, NJ ;
Oinn, TM ;
Pagni, M ;
Servant, F ;
Sigrist, CJA ;
Zdobnov, EM .
NUCLEIC ACIDS RESEARCH, 2001, 29 (01) :37-40
[3]   THE ANTISENSE HOMOLOGY BOX - A NEW MOTIF WITHIN PROTEINS THAT ENCODES BIOLOGICALLY-ACTIVE PEPTIDES [J].
BARANYI, L ;
CAMPBELL, W ;
OHSHIMA, K ;
FUJIMOTO, S ;
BOROS, M ;
OKADA, H .
NATURE MEDICINE, 1995, 1 (09) :894-901
[4]  
Bateman A, 2004, NUCLEIC ACIDS RES, V32, pD138, DOI [10.1093/nar/gkp985, 10.1093/nar/gkh121, 10.1093/nar/gkr1065]
[5]   HYDROPATHIC ANTI-COMPLEMENTARITY OF AMINO-ACIDS BASED ON THE GENETIC-CODE [J].
BLALOCK, JE ;
SMITH, EM .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1984, 121 (01) :203-207
[6]   GENETIC ORIGINS OF PROTEIN SHAPE AND INTERACTION RULES [J].
BLALOCK, JE .
NATURE MEDICINE, 1995, 1 (09) :876-878
[7]   G-ACCUMULATION AND C-ACCUMULATION AT SILENT POSITIONS OF CODONS PRODUCES ADDITIONAL ORFS [J].
BOLDOGKOI, Z ;
MURVAI, J ;
FODOR, I .
TRENDS IN GENETICS, 1995, 11 (04) :125-126
[8]   OPEN READING FRAMES IN THE ANTISENSE STRANDS OF GENES-CODING FOR GLYCOLYTIC-ENZYMES IN SACCHAROMYCES-CEREVISIAE [J].
BOLES, E ;
ZIMMERMANN, FK .
MOLECULAR & GENERAL GENETICS, 1994, 243 (04) :363-368
[9]   INTRINSIC AND EXTRINSIC APPROACHES FOR DETECTING GENES IN A BACTERIAL GENOME [J].
BORODOVSKY, M ;
RUDD, KE ;
KOONIN, EV .
NUCLEIC ACIDS RESEARCH, 1994, 22 (22) :4756-4767
[10]   SIMILARITY BETWEEN THE CORTICOTROPIN (ACTH) RECEPTOR AND A PEPTIDE ENCODED BY AN RNA THAT IS COMPLEMENTARY TO ACTH MESSENGER-RNA [J].
BOST, KL ;
SMITH, EM ;
BLALOCK, JE .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1985, 82 (05) :1372-1375