Comparison of regulatory and structural regions of the Xenopus laevis small heat-shock protein-encoding gene family.
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.
Krone
P H
PH
Department of Biology, University of Waterloo, Ontario, Canada.
Snow
A
A
Ali
A
A
Pasternak
J J
JJ
Heikkila
J J
JJ
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003459:Crystallins / Q000737:chemistry; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D005810:Multigene Family / Q000235:genetics*; D009690:Nucleic Acid Conformation; D011401:Promoter Regions, Genetic / Q000235:genetics; D016415:Sequence Alignment; D014982:Xenopus laevis / Q000235:genetics*
D003459:Crystallins; D006360:Heat-Shock Proteins