The relationship of protein conservation and sequence length

被引:116
作者
Lipman, David J. [1 ]
Souvorov, Alexander [1 ]
Koonin, Eugene V. [1 ]
Panchenko, Anna R. [1 ]
Tatusova, Tatiana A. [1 ]
机构
[1] NIH, Natl Ctr Biotechnol Informat, Bethesda, MD 20894 USA
关键词
Length Distribution; General Constraint; Short Protein; Contact Density; Annotation Artifact;
D O I
10.1186/1471-2148-2-20
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Background: In general, the length of a protein sequence is determined by its function and the wide variance in the lengths of an organism's proteins reflects the diversity of specific functional roles for these proteins. However, additional evolutionary forces that affect the length of a protein may be revealed by studying the length distributions of proteins evolving under weaker functional constraints. Results: We performed sequence comparisons to distinguish highly conserved and poorly conserved proteins from the bacterium Escherichia coli, the archaeon Archaeoglobus fulgidus, and the eukaryotes Saccharomyces cerevisiae, Drosophila melanogaster, and Homo sapiens. For all organisms studied, the conserved and nonconserved proteins have strikingly different length distributions. The conserved proteins are, on average, longer than the poorly conserved ones, and the length distributions for the poorly conserved proteins have a relatively narrow peak, in contrast to the conserved proteins whose lengths spread over a wider range of values. For the two prokaryotes studied, the poorly conserved proteins approximate the minimal length distribution expected for a diverse range of structural folds. Conclusions: There is a relationship between protein conservation and sequence length. For all the organisms studied, there seems to be a significant evolutionary trend favoring shorter proteins in the absence of other, more specific functional constraints.
引用
收藏
页数:10
相关论文
共 19 条
  • [1] Metabolic efficiency and amino acid composition in the proteomes of Escherichia coli and Bacillus subtilis
    Akashi, H
    Gojobori, T
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (06) : 3695 - 3700
  • [2] Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    Altschul, SF
    Madden, TL
    Schaffer, AA
    Zhang, JH
    Zhang, Z
    Miller, W
    Lipman, DJ
    [J]. NUCLEIC ACIDS RESEARCH, 1997, 25 (17) : 3389 - 3402
  • [3] Selection for short introns in highly expressed genes
    Castillo-Davis, CI
    Mekhedov, SL
    Hartl, DL
    Koonin, EV
    Kondrashov, FA
    [J]. NATURE GENETICS, 2002, 31 (04) : 415 - 418
  • [4] Biology's new Rosetta stone
    Das, S
    Yu, LH
    Gaitatzes, C
    Rogers, R
    Freeman, J
    Bienkowska, J
    Adams, RM
    Smith, TF
    Lindellen, J
    [J]. NATURE, 1997, 385 (6611) : 29 - 30
  • [5] GALPERIN MY, 1999, ORG PROKARYOTIC GENO
  • [6] MECHANISMS OF SPONTANEOUS MUTATION IN DNA REPAIR-PROFICIENT ESCHERICHIA-COLI
    HALLIDAY, JA
    GLICKMAN, BW
    [J]. MUTATION RESEARCH, 1991, 250 (1-2): : 55 - 71
  • [7] Protein folding - Molecular chaperones in the cytosol: from nascent chain to folded protein
    Hartl, FU
    Hayer-Hartl, M
    [J]. SCIENCE, 2002, 295 (5561) : 1852 - 1858
  • [8] Protein dispensability and rate of evolution
    Hirsh, AE
    Fraser, HB
    [J]. NATURE, 2001, 411 (6841) : 1046 - 1049
  • [9] Essential genes are more evolutionarily conserved than are nonessential genes in bacteria
    Jordan, IK
    Rogozin, IB
    Wolf, YI
    Koonin, EV
    [J]. GENOME RESEARCH, 2002, 12 (06) : 962 - 968
  • [10] Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi
    Katinka, MD
    Duprat, S
    Cornillot, E
    Méténier, G
    Thomarat, F
    Prensier, G
    Barbe, V
    Peyretaillade, E
    Brottier, P
    Wincker, P
    Delbac, F
    El Alaoui, H
    Peyret, P
    Saurin, W
    Gouy, M
    Weissenbach, J
    Vivarès, CP
    [J]. NATURE, 2001, 414 (6862) : 450 - 453