Extracting sequence motifs and the phylogenetic features of SNARE-dependent membrane traffic

被引:45
作者
Yoshizawa, Akiyasu C. [1 ]
Kawashima, Shuichi
Okuda, Shujiro
Fujita, Masashi
Itoh, Masumi
Moriya, Yuki
Hattori, Masahiro
Kanehisa, Minoru
机构
[1] Kyoto Univ, Inst Chem Res, Bioinformat Ctr, Kyoto 6110011, Japan
[2] Univ Tokyo, Inst Med Sci, Ctr Human Genome, Minato Ku, Tokyo 1088639, Japan
关键词
bioinformatics; comparative genomics; membrane traffic; phylogenetic analysis; sequence motif; SNARE proteins; vesicular transport;
D O I
10.1111/j.1600-0854.2006.00451.x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The SNARE proteins are required for membrane fusion during intracellular vesicular transport and for its specificity. Only the unique combination of SNARE proteins (cognates) can be bound and can lead to membrane fusion, although the characteristics of the possible specificity of the binding combinations encoded in the SNARE sequences have not yet been determined. We discovered by whole genome sequence analysis that sequence motifs (conserved sequences) in the SNARE motif domains for each protein group correspond to localization sites or transport pathways. We claim that these motifs reflect the specificity of the binding combinations of SNARE motif domains. Using these motifs, we could classify SNARE proteins from 48 organisms into their localization sites or transport pathways. The classification result shows that more than 10 SNARE subgroups are kingdom specific and that the SNARE paralogs involved in the plasma membrane-related transport pathways have developed greater variations in higher animals and higher plants than those involved in the endoplasmic reticulum-related transport pathways throughout eukaryotic evolution.
引用
收藏
页码:1104 / 1118
页数:15
相关论文
共 63 条
[11]   Use1p is a yeast SNARE protein required for retrograde traffic to the ER [J].
Dilcher, M ;
Veith, B ;
Chidambaram, S ;
Hartmann, E ;
Schmitt, HD ;
von Mollard, GF .
EMBO JOURNAL, 2003, 22 (14) :3664-3674
[12]   Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6 [J].
Dilcher, M ;
Köhler, B ;
von Mollard, GF .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (37) :34537-34544
[13]   Profile hidden Markov models [J].
Eddy, SR .
BIOINFORMATICS, 1998, 14 (09) :755-763
[14]   The PROSITE database, its status in 2002 [J].
Falquet, L ;
Pagni, M ;
Bucher, P ;
Hulo, N ;
Sigrist, CJA ;
Hofmann, K ;
Bairoch, A .
NUCLEIC ACIDS RESEARCH, 2002, 30 (01) :235-238
[15]   Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs [J].
Fasshauer, D ;
Sutton, RB ;
Brunger, AT ;
Jahn, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (26) :15781-15786
[16]  
Felsenstein J., 2005, PHYLIP PHYLOGENY INF, DOI DOI 10.1111/J.1096-0031.1989.TB00562.X
[17]   Functional architecture of an intracellular membrane t-SNARE [J].
Fukuda, R ;
McNew, JA ;
Weber, T ;
Parlati, F ;
Engel, T ;
Nickel, W ;
Rothman, JE ;
Söllner, TH .
NATURE, 2000, 407 (6801) :198-202
[18]   The yeast endosomal t-SNARE, pep12p, functions in the absence of its transmembrane domain [J].
Gerrard, SR ;
Mecklem, AB ;
Stevens, TH .
TRAFFIC, 2000, 1 (01) :45-55
[19]   Pep12p is a multifunctional yeast syntaxin that controls entry of biosynthetic, endocytic and retrograde traffic into the prevacuolar compartment [J].
Gerrard, SR ;
Levi, BP ;
Stevens, TH .
TRAFFIC, 2000, 1 (03) :259-269
[20]   Cell biology of the primitive eukaryote Giardia lamblia [J].
Gillin, FD ;
Reiner, DS ;
McCaffery, JM .
ANNUAL REVIEW OF MICROBIOLOGY, 1996, 50 :679-705