The structure and expression of a distantly related member of the beta-gamma crystallin super gene family from Xenopus.
In an attempt to understand amphibian crystallin gene regulation, we have isolated and partially characterized several genomic clones which hybridized to the gamma 1 cDNA probe from Rana temporaria. A complete sequence of one of these clones showed slight homology to the mammalian beta and gamma crystallins. The deduced amino acid sequence of the coding region and its alignment as a folding unit indicated that all the topologically equivalent residues involved in maintaining the protein folding pattern are highly conserved. Northern blot analysis of total RNAs derived from several adult tissues, including eye lens, suggested that an RNA of approximately 700 nucleotides long is present in lens, heart, spleen and embryos of later stages of development but not in retina, oocytes and embryos of early developmental stages.
Eye Research Institute, Oakland University, Rochester, Michigan 48309.
B S
BS
Shastry
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Reddy
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D003459:Crystallins / Q000235:genetics*; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D015870:Gene Expression; D007908:Lens, Crystalline / Q000378:metabolism; D008969:Molecular Sequence Data; D005810:Multigene Family; D010957:Plasmids; D012313:RNA / Q000235:genetics / Q000302:isolation & purification; D011896:Rana temporaria; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D014982:Xenopus laevis
D003459:Crystallins; D012313:RNA; D004247:DNA