Chloroplast small heat shock proteins: Evidence for atypical evolution of an organelle-localized protein

Knowledge of the origin and evolution of gene families is critical to our u nderstanding of the evolution of protein function. To gain a detailed under standing of the evolution of the small heat shock proteins (sHSPs) in plant s, we have examined the evolutionary history of the chloroplast (CP)-locali zed sHSPs. Previously, these nuclear-encoded CP proteins had been identifie d only from angiosperms. This study reveals the presence of the CP sHSPs in a moss, Funaria hygrometrica. Two clones for CP sHSPs were isolated from a F. hygrometrica heat shock cDNA library that represent two distinct CP sHS P genes. Our analysis of the CP sHSPs reveals unexpected evolutionary relat ionships and patterns of sequence conservation. Phylogenetic analysis of th e CP sHSPs with other plant CP sHSPs and eukaryotic, archaeal, and bacteria l sHSPs shows that the CP sHSPs are not closely related to the cyanobacteri al sHSPs. Thus, they most likely evolved via gene duplication from a nuclea r-encoded cytosolic sHSP and not via gene transfer from the CP endosymbiont . Previous sequence analysis had shown that all angiosperm CP sHSPs possess a methionine-rich region in the N-terminal domain. The primary sequence of this region is not highly conserved in the F, hygrometrica CP sHSPs. This lack of sequence conservation indicates that sometime in land plans evoluti on, after the divergence of mosses from the common ancestor of angiosperms but before the monocot-dicot divergence, there was a change in the selectiv e constraints acting on the CP sHSPs.