Linked Life Data

7575513

Source:http://linkedlifedata.com/resource/pubmed/id/7575513

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-11-2
pubmed:databankReference
pubmed:abstractText
rho-Crystallin is a major enzyme crystallin present in the lenses of amphibian species with a blocked amino terminus. In order to facilitate the determination of the primary sequence of this taxon-specific crystallin, cDNA mixture was synthesized from the poly(A)+mRNA of bullfrog eye lenses. cDNAs encoding rho-crystallin were then amplified by polymerase chain reaction (PCR) using a new protocol of Rapid Amplification of cDNA Ends (RACE). PCR-amplified product corresponding to rho-crystallin was obtained, which was then subcloned into pUC18 vector and then transformed into E. coli strain JM109. Plasmids purified from the positive clones were prepared for nucleotide sequencing by the automatic fluorescence-based dideoxynucleotide chain-termination method. Sequencing more than 15 clones containing DNA inserts coding for rho-crystallin constructed only one unique and complete full-length reading frame of 975 base pairs covering a deduced protein sequence of 324 amino acids including the universal initiating methionine. It shows 96, 59, 46 and 37 percent sequence similarity to another rho-crystallin from European common frog, bovine prostaglandin-F synthase, human aldose reductase and human aldehyde reductase, respectively, revealing the close relationship between rho-crystallins from related amphibian species and its possible evolutionary relatedness with various aldo-keto reductases. In this study a phylogenetic tree for rho-crystallin and related enzymes is constructed based on multiple-sequence alignment program using a combination of distance matrix and approximate parsimony methods. We have thus established the remote phylogenetic relationship between rho-crystallin and some aldehyde/aldose reductases, which may provide a possible link for the recruitment of this crystallin from detoxification-related enzymes and its physiological role in maintaining a transparent and clear lens.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
214
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1079-88
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7575513-Alcohol Oxidoreductases, pubmed-meshheading:7575513-Amino Acid Sequence, pubmed-meshheading:7575513-Animals, pubmed-meshheading:7575513-Base Sequence, pubmed-meshheading:7575513-Cattle, pubmed-meshheading:7575513-Cloning, Molecular, pubmed-meshheading:7575513-Crystallins, pubmed-meshheading:7575513-DNA, Complementary, pubmed-meshheading:7575513-DNA Primers, pubmed-meshheading:7575513-Humans, pubmed-meshheading:7575513-Molecular Sequence Data, pubmed-meshheading:7575513-Phylogeny, pubmed-meshheading:7575513-Polymerase Chain Reaction, pubmed-meshheading:7575513-RNA, Messenger, pubmed-meshheading:7575513-Rana catesbeiana, pubmed-meshheading:7575513-Rana temporaria, pubmed-meshheading:7575513-Recombinant Proteins, pubmed-meshheading:7575513-Sequence Homology, Amino Acid
pubmed:year
1995
pubmed:articleTitle
Sequence analysis of frog rho-crystallin by cDNA cloning and sequencing: a member of the aldo-keto reductase family.
pubmed:affiliation
Laboratory of Crystallin Research, National Taiwan University, Taipei.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't