Comparative genomics reveals selective distribution and domain organization of FYVE and PX domain proteins across eukaryotic lineages

被引:15
作者
Banerjee, Sumana [2 ]
Basu, Soumalee [1 ]
Sarkar, Srimonti [2 ]
机构
[1] W Bengal Univ Technol, Sch Biotechnol, Dept Biotechnol, Kolkata 700064, India
[2] Indian Inst Sci Educ & Res, Dept Biol Sci, Nadia 741252, W Bengal, India
关键词
MEMBRANE-BINDING ANALYSIS; PHOX HOMOLOGY DOMAIN; PHOSPHATIDYLINOSITOL; 3-PHOSPHATE; ENDOSOMAL LOCALIZATION; ARABIDOPSIS-THALIANA; PHOSPHOINOSITIDES; IDENTIFICATION; RECOGNITION; EVOLUTION; DOCKING;
D O I
10.1186/1471-2164-11-83
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Background: Phosphatidylinositol 3-phosphate is involved in regulation of several key cellular processes, mainly endocytosis, signaling, nuclear processes, cytoskeletal remodelling, cell survival, membrane trafficking, phagosome maturation and autophagy. In most cases effector proteins bind to this lipid, using either FYVE or PX domain. These two domains are distributed amongst varied life forms such as virus, protists, fungi, viridiplantae and metazoa. As the binding ligand is identical for both domains, the goal of this study was to understand if there is any selectivity for either of these domains in different taxa. Further, to understand the different cellular functions that these domains may be involved in, we analyzed the taxonomic distribution of additional domains that associate with FYVE and PX. Results: There is selectivity for either FYVE or PX in individual genomes where both domains are present. Fungi and metazoa encode more PX, whereas streptophytes in viridiplantae encode more FYVE. Excess of FYVE in streptophytes results from proteins containing RCC1 and DZC domains and FYVE domains in these proteins have a non-canonical ligand-binding site. Within a taxonomic group the selected domain associates with a higher number of other domains and is thus expected to discharge a larger number of cellular functions. Also, while certain associated domains are present in all taxonomic groups, most of them are unique to a specific group indicating that while certain common functions are discharged by these domains in all taxonomic groups, some functions appear to be group specific. Conclusions: Although both FYVE and PX bind to PtdIns(3) P, genomes of different taxa show distinct selectivity of encoding either of the two. Higher numbers of taxonomic group specific domains co-occur with the more abundant domain (FYVE/PX) indicating that group-specific rare domain architectures might have emerged to accomplish certain group-specific functions.
引用
收藏
页数:12
相关论文
共 46 条
[1]   Evolution of protein domain promiscuity in eukaryotes [J].
Basu, Malay Kumar ;
Carmel, Liran ;
Rogozin, Igor B. ;
Koonin, Eugene V. .
GENOME RESEARCH, 2008, 18 (03) :449-461
[2]   The crystal structure of the PX domain from p40phox bound to phosphatidylinositol 3-phosphate [J].
Bravo, J ;
Karathanassis, D ;
Pacold, CM ;
Pacold, ME ;
Ellson, CD ;
Anderson, KE ;
Butler, PJG ;
Lavenir, I ;
Perisic, O ;
Hawkins, PT ;
Stephens, L ;
Williams, RL .
MOLECULAR CELL, 2001, 8 (04) :829-839
[3]   Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains [J].
Burd, CG ;
Emr, SD .
MOLECULAR CELL, 1998, 2 (01) :157-162
[4]   NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the phox homology (PX) domain [J].
Cheng, GJ ;
Lambeth, JD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (06) :4737-4742
[5]   Modular phosphoinositide-binding domains - their role in signalling and membrane trafficking [J].
Cullen, PJ ;
Cozier, GE ;
Banting, G ;
Mellor, H .
CURRENT BIOLOGY, 2001, 11 (21) :R882-R893
[6]   RCC1 IN THE CELL-CYCLE - THE REGULATOR OF CHROMOSOME CONDENSATION TAKES ON NEW ROLES [J].
DASSO, M .
TRENDS IN BIOCHEMICAL SCIENCES, 1993, 18 (03) :96-101
[7]   PI-loting membrane traffic [J].
De Matteis, MA ;
Godi, A .
NATURE CELL BIOLOGY, 2004, 6 (06) :487-492
[8]   Genome analysis of the smallest free-living eukaryote Ostreococcus tauri unveils many unique features [J].
Derelle, Evelyne ;
Ferraz, Conchita ;
Rombauts, Stephane ;
Rouze, Pierre ;
Worden, Alexandra Z. ;
Robbens, Steven ;
Partensky, Frederic ;
Degroeve, Sven ;
Echeynie, Sophie ;
Cooke, Richard ;
Saeys, Yvan ;
Wuyts, Jan ;
Jabbari, Kamel ;
Bowler, Chris ;
Panaud, Olivier ;
Piegu, Benoit ;
Ball, Steven G. ;
Ral, Jean-Philippe ;
Bouget, Francois-Yves ;
Piganeau, Gwenael ;
De Baets, Bernard ;
Picard, Andre ;
Delseny, Michel ;
Demaille, Jacques ;
Van de Peer, Yves ;
Moreau, Herve .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (31) :11647-11652
[9]   INOSITIDES AND THE NUCLEUS AND INOSITIDES IN THE NUCLEUS [J].
DIVECHA, N ;
BANFIC, H ;
IRVINE, RF .
CELL, 1993, 74 (03) :405-407
[10]   Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities [J].
Dowler, S ;
Currie, RA ;
Campbell, DG ;
Deak, M ;
Kular, G ;
Downes, CP ;
Alessi, DR .
BIOCHEMICAL JOURNAL, 2000, 351 (01) :19-31