Boreskov

PP‐12Comparison of molecular evolution model of the GTF2I family with real data usingmethod implemented in SAMEM [3] discovered several types of statistically rare aminoacidsreplacements (p≤0.01) which characterized by greatest physicochemical changes. Thesereplacements related with: 1) the divergence between gtf2ird1 R4 and gtf2i R6, 2) the originof gtf2ird1 R1 and R2 ancestor, and 3) the origin of gtf2ird1 R1 and gtf2i R1 ancestor. Weused the program package PDB3DScan for structural alignment to find the differences in the3D structure of GTF2I repeats in gtf2i, gtf2ird1 and gtf2ird2 genes and identified that thosestatistically rare substitution mostly situated in loop regions or in the beginning or in the endof helices. We showed that the helix in structure of the first repeat of gtf2i, gtf2ird1, gtf2ird2is much less conservative then in the other repeats. We also found the unique mutationalpattern for each GTF2I repeat that could be caused by their functional specialization (forexample, DNA‐binding [4]).This work was supported by RFBR grant No. 09‐04‐01641‐a and Biosphere Origin andEvolution program.References[1]. Bayarsaihan, D. et al. (2002) Genomic organization of the genes Gtf2ird1, Gtf2i, and Ncf1 at the mousechromosome 5 region syntenic to the human chromosome 7q11.23 Williams syndrome critical region,Genomics, 79:137‐143.[2]. P. Dehal, J.L Boore. (2005) Two Rounds of Whole Genome Duplication in the Ancestral Vertebrate, PLoSBiol., 3:e314.[3]. K.V. Gunbin et al. (2010) A computer system for the analysis of molecular evolution modes of proteinencodinggenes (SAMEM), Moscow University Biological Sciences Bulletin, 65:142‐144.[4]. S.J. Palmer et al. (2010) Negative autoregulation of GTF2IRD1 in Williams‐Beuren syndrome via a novelDNA binding mechanism, J. Biol. Chem., 285:4715‐4724.152