Gene 1992 Jan 15;1102:159-66.

Comparison of regulatory and structural regions of the Xenopus laevis small heat-shock protein-encoding gene family.

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We have isolated several unique Xenopus laevis hsp30 (encoding heat-shock protein 30) genomic clones, one of which contains two complete hsp30 genes (hsp30C and hsp30D), as well as the promoter and N-terminal coding region of a third gene (hsp30E). Nucleotide sequence and restriction enzyme analysis revealed that this gene cluster is different from a cluster isolated previously. The hsp30C and hsp30D genes encode proteins of approx. 24 kDa. In all, the hsp30 gene family contains a minimum of seven genes. The strand exchange and breakage of the duplication events which generated this gene family appear to have occurred within tracts of DNA which potentially can assume a Z-DNA conformation. Comparing the amino acid (aa) sequences of each known Hsp30 protein with bovine alpha-crystallin revealed a high degree of shared conservation of aa that constitute the major structural feature(s) of alpha-crystallin.

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Species referenced: Xenopus laevis
Genes referenced: hsp30c hsp30d hsp30e