MBE Advance Access published online on April 14, 2004
Molecular Biology and Evolution, doi:10.1093/molbev/msh146
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved
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1 International Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland
* To whom correspondence should be addressed. E-mail: grzesiek{at}iimcb.gov.pl.
To investigate the mechanisms regulating the nucleotide usage in mammalian genes, we analysed the sequences of three physically linked Hsp70 paralogs in human and mouse. We report that the sequences of HSPA1A and HSPA1B genes are almost identical, whereas the HSPA1L gene contains some regions very similar to HSPA1A/B, and some regions with much higher divergence. Phylogenetic analysis reveals that gene conversion has homogenised the entire coding regions of HSPA1A/B and several fragments of HSPA1L. The regions undergoing conversion are all very GC-rich, contrarily to the regions not subject to conversion. The pattern of nucleotide substitution in mammalian orthologs suggests that the mechanism increasing the GC content is still functioning. To test the possibility that the high GC content facilitates the expression of Hsp70 during heat-shock, we performed in vitro translation experiments. We failed to detect any effect of GC content on the translation efficiency at high temperatures. Taken together, our data strongly support the biased gene conversion hypothesis of GC content evolution. Key Words:
GC content, gene conversion, heat-shock
Original Articles
Gene Conversion and GC Content Evolution in Mammalian Hsp70
2 Institute of Biochemistry and Biophysics, 02-106 Warsaw, Poland
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