Formin homology 2 domains occur in multiple contexts in angiosperms -: art. no. 44

被引:83
作者
Cvrcková, F
Novotny, M
Pícková, D
Zársky, V
机构
[1] Charles Univ Prague, Fac Sci, Dept Plant Physiol, CZ-12844 Prague 2, Czech Republic
[2] Uppsala Univ, Ctr Biomed, Dept Cell & Mol Biol, S-75123 Uppsala, Sweden
[3] Fac Sci Czech Republ, Inst Expt Bot, CZ-16502 Prague 6, Czech Republic
关键词
D O I
10.1186/1471-2164-5-44
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: Involvement of conservative molecular modules and cellular mechanisms in the widely diversified processes of eukaryotic cell morphogenesis leads to the intriguing question: how do similar proteins contribute to dissimilar morphogenetic outputs. Formins (FH2 proteins) play a central part in the control of actin organization and dynamics, providing a good example of evolutionarily versatile use of a conserved protein domain in the context of a variety of lineage-specific structural and signalling interactions. Results: In order to identify possible plant-specific sequence features within the FH2 protein family, we performed a detailed analysis of angiosperm formin-related sequences available in public databases, with particular focus on the complete Arabidopsis genome and the nearly finished rice genome sequence. This has led to revision of the current annotation of half of the 22 Arabidopsis formin-related genes. Comparative analysis of the two plant genomes revealed a good conservation of the previously described two subfamilies of plant formins ( Class I and Class II), as well as several subfamilies within them that appear to predate the separation of monocot and dicot plants. Moreover, a number of plant Class II formins share an additional conserved domain, related to the protein phosphatase/tensin/auxilin fold. However, considerable inter-species variability sets limits to generalization of any functional conclusions reached on a single species such as Arabidopsis. Conclusions: The plant-specific domain context of the conserved FH2 domain, as well as plant-specific features of the domain itself, may reflect distinct functional requirements in plant cells. The variability of formin structures found in plants far exceeds that known from both fungi and metazoans, suggesting a possible contribution of FH2 proteins in the evolution of the plant type of multicellularity.
引用
收藏
页数:18
相关论文
共 85 条
[1]   Diaphanous-related Formin homology proteins [J].
Alberts, AS .
CURRENT BIOLOGY, 2002, 12 (23) :R796-R796
[2]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[3]  
[Anonymous], 2002, Genome Biol
[4]  
[Anonymous], 2004, SEQUENCE MANIPULATIO
[5]  
Banno H, 2000, PLANT CELL PHYSIOL, V41, P617, DOI 10.1093/pcp/41.5.617
[6]   CRYSTAL-STRUCTURE OF HUMAN PROTEIN-TYROSINE-PHOSPHATASE 1B [J].
BARFORD, D ;
FLINT, AJ ;
TONKS, NK .
SCIENCE, 1994, 263 (5152) :1397-1404
[7]   Prediction of complete gene structures in human genomic DNA [J].
Burge, C ;
Karlin, S .
JOURNAL OF MOLECULAR BIOLOGY, 1997, 268 (01) :78-94
[8]  
BURGE CB, 1998, COMPUTATIONAL METHOD, P127
[9]  
CASTRILLON DH, 1994, DEVELOPMENT, V120, P3367
[10]   Movement of a cytokinesis factor cdcl2p to the site of cell division [J].
Chang, F .
CURRENT BIOLOGY, 1999, 9 (15) :849-852