Sequence analysis of one major basic β-crystallin (β-Bp) of amphibian lenses: Evolutionary comparison and phylogenetic relatedness between β-crystallin and γ-crystallin

Fu Ming Pan, Wen Chang Chang, Shao Fan Lu, Ao Lin Hsu, Shyh Horng Chiou

研究成果: 雜誌貢獻文章

7 引文 (Scopus)

摘要

βBp-Crystailin a major basic β-crystallin of vertebrate eye lens, is developmentally regulated during the process of amphibian metamorphosis. In order to facilitate the determination of the primary sequence of this ubiquitous crystallin present in all vertebrate species, cDNA mixture was synthesized from the poly(A)+ mRNA isolated from bullfrog eye lenses. A protocol of Rapid Amplification of cDNA Ends (RACE) was used to amplify cDNAs encoding βBp-crystallin by polymerase chain reaction (PCR). PCR-amplified product corresponding to βBp-crystallin was then ligated into pGEM-T vector and then transformed into E. coli strain JM109. One complete full-length reading frame of 615 base pairs, which covers a deduced protein sequence of 205 amino acids, including the universal initiating methionine, was revealed by automatic nucleotide sequencing with a fluorescence-based dideoxynucleotide chain-termination method. It shows 83, 74, 78 and 80 percent sequence similarity to the homologous β2 crystallins of chicken, rat, bovine, and human species, respectively, revealing the close structural relationship among βBp-crystallins even from remotely related species. In this study phylogenetic trees based on nucleotide and protein sequences of various β- and γ-crystallins from different vertebrate classes are constructed using a combination of distance matrix and approximate parsimony methods. which corroborate the previous supposition that β- and γ-crystallins form a superfamily with a common ancestry.
原文英語
頁(從 - 到)940-949
頁數10
期刊Biochemical and Biophysical Research Communications
217
發行號3
DOIs
出版狀態已發佈 - 十二月 26 1995
對外發佈Yes

指紋

Crystallins
Amphibians
Lenses
Sequence Analysis
Vertebrates
Crystalline Lens
Complementary DNA
Polymerase chain reaction
Nucleotides
Dideoxynucleotides
Rana catesbeiana
Reading Frames
Polymerase Chain Reaction
Base Pairing
Methionine
Escherichia coli
Amplification
Rats
Amino Acid Sequence
Chickens

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

引用此文

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title = "Sequence analysis of one major basic β-crystallin (β-Bp) of amphibian lenses: Evolutionary comparison and phylogenetic relatedness between β-crystallin and γ-crystallin",
abstract = "βBp-Crystailin a major basic β-crystallin of vertebrate eye lens, is developmentally regulated during the process of amphibian metamorphosis. In order to facilitate the determination of the primary sequence of this ubiquitous crystallin present in all vertebrate species, cDNA mixture was synthesized from the poly(A)+ mRNA isolated from bullfrog eye lenses. A protocol of Rapid Amplification of cDNA Ends (RACE) was used to amplify cDNAs encoding βBp-crystallin by polymerase chain reaction (PCR). PCR-amplified product corresponding to βBp-crystallin was then ligated into pGEM-T vector and then transformed into E. coli strain JM109. One complete full-length reading frame of 615 base pairs, which covers a deduced protein sequence of 205 amino acids, including the universal initiating methionine, was revealed by automatic nucleotide sequencing with a fluorescence-based dideoxynucleotide chain-termination method. It shows 83, 74, 78 and 80 percent sequence similarity to the homologous β2 crystallins of chicken, rat, bovine, and human species, respectively, revealing the close structural relationship among βBp-crystallins even from remotely related species. In this study phylogenetic trees based on nucleotide and protein sequences of various β- and γ-crystallins from different vertebrate classes are constructed using a combination of distance matrix and approximate parsimony methods. which corroborate the previous supposition that β- and γ-crystallins form a superfamily with a common ancestry.",
author = "Pan, {Fu Ming} and Chang, {Wen Chang} and Lu, {Shao Fan} and Hsu, {Ao Lin} and Chiou, {Shyh Horng}",
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T1 - Sequence analysis of one major basic β-crystallin (β-Bp) of amphibian lenses

T2 - Evolutionary comparison and phylogenetic relatedness between β-crystallin and γ-crystallin

AU - Pan, Fu Ming

AU - Chang, Wen Chang

AU - Lu, Shao Fan

AU - Hsu, Ao Lin

AU - Chiou, Shyh Horng

PY - 1995/12/26

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AB - βBp-Crystailin a major basic β-crystallin of vertebrate eye lens, is developmentally regulated during the process of amphibian metamorphosis. In order to facilitate the determination of the primary sequence of this ubiquitous crystallin present in all vertebrate species, cDNA mixture was synthesized from the poly(A)+ mRNA isolated from bullfrog eye lenses. A protocol of Rapid Amplification of cDNA Ends (RACE) was used to amplify cDNAs encoding βBp-crystallin by polymerase chain reaction (PCR). PCR-amplified product corresponding to βBp-crystallin was then ligated into pGEM-T vector and then transformed into E. coli strain JM109. One complete full-length reading frame of 615 base pairs, which covers a deduced protein sequence of 205 amino acids, including the universal initiating methionine, was revealed by automatic nucleotide sequencing with a fluorescence-based dideoxynucleotide chain-termination method. It shows 83, 74, 78 and 80 percent sequence similarity to the homologous β2 crystallins of chicken, rat, bovine, and human species, respectively, revealing the close structural relationship among βBp-crystallins even from remotely related species. In this study phylogenetic trees based on nucleotide and protein sequences of various β- and γ-crystallins from different vertebrate classes are constructed using a combination of distance matrix and approximate parsimony methods. which corroborate the previous supposition that β- and γ-crystallins form a superfamily with a common ancestry.

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