NDLI: Sequence Characterization of γ-Crystallins from Lip Shark (Chiloscyllium colax): Existence of Two cDNAs Encoding γ-Crystallins of Mammalian and Teleostean Classes

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Sequence Characterization of γ-Crystallins from Lip Shark (Chiloscyllium colax): Existence of Two cDNAs Encoding γ-Crystallins of Mammalian and Teleostean Classes

Physical and Epitope Analysis of a Recombinant Human T-Cell Receptor Vα/Vβ Construct Support the Similarity to Immunoglobulin

The Protein Journal : Volume 16, Issue 3, April 1997

The Protein Journal : Volume 16, Issue 2, February 1997

The Protein Journal : Volume 16, Issue 1, January 1997

Sequence Characterization of γ-Crystallins from Lip Shark (Chiloscyllium colax): Existence of Two cDNAs Encoding γ-Crystallins of Mammalian and Teleostean Classes

Content Provider	Springer Nature Link
Author	Chuang, Ming Hong Pan, Fu Ming Chiou, Shyh Horng
Copyright Year	1997
Abstract	γ-Crystallin is a common lens protein of most vertebrate eye lenses and the major protein component in lenses of fishes and in many mammalian species during embryonic and neonatal stages. To facilitate the structural characterization of γ-crystallin possessing extensive charge heterogeneity, a cDNA mixture was constructed from the poly(A)$^{+}$ mRNA isolated from shark eye lenses, and amplification by polymerase chain reaction (PCR) was carried out to obtain cDNAs encoding multiple shark γ-crystallins. Sequencing analysis of multiple positive clones containing PCR-amplified inserts revealed the presence of a multiplicity of isoforms in the γ-crystallin class of this cartilaginous fish. It was of interest to find that two shark cDNA sequences coexist, one encoding γ-crystallin (γM$_{1}$) of high methionine content (15.5%) and the other encoding one (γM$_{2}$) of low methionine content (5.1%), each corresponding to the major teleostean and mammalian γ-crystallins, respectively. Comparison of protein sequences encoded by these two shark cDNAs with published sequences of γ-crystallins from mouse, bovine, human, frog, and carp lenses indicated that there is about 61–80% sequence homology between different species of the piscine class, whereas only 47–66% is found between mammals and shark. A phylogenetic tree constructed on the basis of sequence divergence among various γ-crystallin cDNAs revealed the close relatedness between shark γM$_{2}$-crystallin and mammalian γ-crystallins and that between shark γM$_{1}$ and teleostean γ-crystallins. The results pointed to the fact that ancestral precursors of γ-crystallins were present in the sharp lens long before the appearance of modern-day mammalian and teleostean γ-crystallins.
Starting Page	299
Ending Page	307
Page Count	9
File Format	PDF
ISSN	02778033
Journal	The Protein Journal
Volume Number	16
Issue Number	4
e-ISSN	15734943
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	1997-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Organic Chemistry Bioorganic Chemistry Biochemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Biochemistry

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