The extant core bacterial proteome is an archive of the origin of life

被引:39
作者
Danchin, Antoine [1 ]
Fang, Gang [1 ]
Noria, Stanislas [1 ]
机构
[1] Inst Pasteur, F-75724 Paris, France
关键词
homeotopic transformation; oxygen toxicity; paleocells; synthetic biology; YycF;
D O I
10.1002/pmic.200600442
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Genes consistently present in a clique of genomes, preferring the leading DNA strands are deemed persistent. The persistent bacterial proteome organises around intermediary and RNA metabolism, and RNA-related information transfer, with a significant contribution to compar\tmentalisation. Despite inevitable losses during evolution, the extant persistent proteome displays functions present early on. Proteins coded by genes staying clustered in a majority of genomes constitute a network of mutual attraction made up of three concentric circles. The outer one, mostly devoted to metabolism, breaks into small pieces and fades away. The second, more continuous, one organises around class I tRNA synthetases. The well-connected inner circle comprises the ribosome and information transfer. This reflects the progressive construction of cells, starting from the metabolism of coenzymes, nucleotides and fatty acids-related molecules. Subsequently, a core set of aminoacyl-tRNA synthetases scaffolded around RNA, connected to cell division machinery and organised metabolism around translation. This remarkable organisation reflects the evolution of life from small molecules metabolism to the RNA world, suggesting that extant microorganisms carry the marks of the ancient processes that created life. Further analysis suggests that RNA degradation, associated to the presence of iron, still plays a role in extant metabolism, including the evolution of genome structures.
引用
收藏
页码:875 / 889
页数:15
相关论文
共 65 条
[1]  
[Anonymous], 2003, DELPHIC BOAT WHAT GE
[2]  
[Anonymous], 1993, LOGIC LIFE
[3]   Enzymes of the heme biosynthetic pathway in the nonphotosynthetic alga Polytomella sp. [J].
Atteia, A ;
van Lis, R ;
Beale, SI .
EUKARYOTIC CELL, 2005, 4 (12) :2087-2097
[4]   Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants:: the Keio collection [J].
Baba, Tomoya ;
Ara, Takeshi ;
Hasegawa, Miki ;
Takai, Yuki ;
Okumura, Yoshiko ;
Baba, Miki ;
Datsenko, Kirill A. ;
Tomita, Masaru ;
Wanner, Barry L. ;
Mori, Hirotada .
MOLECULAR SYSTEMS BIOLOGY, 2006, 2 (1) :2006.0008
[5]   NATURAL-SELECTION, PROTEIN ENGINEERING, AND THE LAST RIBOORGANISM - RATIONAL MODEL-BUILDING IN BIOCHEMISTRY [J].
BENNER, SA ;
ALLEMANN, RK ;
ELLINGTON, AD ;
GE, L ;
GLASFELD, A ;
LEANZ, GF ;
KRAUCH, T ;
MACPHERSON, LJ ;
MORONEY, S ;
PICCIRILLI, JA ;
WEINHOLD, E .
COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY, 1987, 52 :53-63
[6]   Aptamer to ribozyme: The intrinsic catalytic potential of a small RNA [J].
Brackett, David M. ;
Dieckmann, Thorsten .
CHEMBIOCHEM, 2006, 7 (05) :839-843
[7]   Clustering of isochorismate synthase genes menF and entC and channeling of isochorismate in Escherichia coli [J].
Buss, K ;
Müller, R ;
Dahm, C ;
Gaitatzis, N ;
Skrzypczak-Pietraszek, E ;
Lohmann, S ;
Gassen, M ;
Leistner, E .
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 2001, 1522 (03) :151-157
[8]  
Cairns-Smith A.G., 1982, Genetic Takeover and the Mineral Origin of Life
[9]   Mechanism of the F1F0-type ATP synthase, a biological rotary motor [J].
Capaldi, RA ;
Aggeler, R .
TRENDS IN BIOCHEMICAL SCIENCES, 2002, 27 (03) :154-160
[10]   The Escherichia coli RNA degradosome:: structure, function and relationship to other ribonucleolytic multienyzme complexes [J].
Carpousis, AJ .
BIOCHEMICAL SOCIETY TRANSACTIONS, 2002, 30 :150-155