IIB   20738
INSTITUTO DE INVESTIGACIONES BIOLOGICAS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
A structure function analysis of sHSPs in plants
Lugar:
Quilmes
Reunión:
Congreso; 1er Congreso Argentino de Bioinformática y Biología Computacional; 2010
Institución organizadora:
Asociación Argentina de Bioinformática y Biología Computacional
Resumen:
BackgroundSmall heat shock proteins (sHSPs) are associated with stress responses among which the heat shockresponse. They are believed to function as molecular chaperones in order to prevent proteins frombeing denatured in extreme conditions. Nonstress roles have also been suggested. sHSPs are ubiquitousin all three domains of life and form a superfamily that consists of many small proteins that have an α-crystallin (AC) domain, which comprise about 100 amino acid residues. The AC domain is involved inpreventing undesirable protein-protein interactions. Genome studies in lower plants indicateconsiderable structural and functional diversity. Recently, a number of higher plant genome sequenceshas become public which allows to elaborate on the previously performed studies in lower plants.ResultsThe genomes of Arabidopsis thaliana, rice, poplar, grape and tomato were mined in order to identifysHSPs. Strong differences in the number of sHSP encoding genes were found. In order to initiate astructure-function prediction analysis, we performed a multiple sequence alignment and phylogeny.Phylogeny showed the existence of a number of orthologous sHSP classes but also species specificparalogs. MEME identified a number of strongly conserved subsequences as well as a number ofsHSPs classes. Results of co-evolution, evolutionary trace and DIVERGE analysis will be discussed interms of both structure and function of the AC domain and sHSPs in plants.ConclusionssHSPs in higher plants form a large and various superfamily of proteins, that given the demonstratedvariance in both sequence and tertiary structure might be involved in many aspects of plants' survival.More studies will be required in order to obtain insight in how sHSP interact with other proteins.