摘要
| 原文 | 英語 |
|---|---|
| 頁（從 - 到） | 226-229 |
| 頁數 | 4 |
| 期刊 | BBA - Gene Structure and Expression |
| 卷 | 951 |
| 發行號 | 1 |
| DOIs | |
| 出版狀態 | 已發佈 - 十一月 10 1988 |
| 對外發佈 | Yes |
指紋
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Genetics
引用此文
Carp gamma-crystallins with high methionine content : Cloning and sequencing of the complementary DNA. / Chang, Tschining; Jiang, Yun Jin; Chiou, Shyh Horng; Chang, Wen Chang.
於: BBA - Gene Structure and Expression, 卷 951, 編號 1, 10.11.1988, p. 226-229.研究成果: 雜誌貢獻 › 文章
}
TY - JOUR
T1 - Carp gamma-crystallins with high methionine content
T2 - Cloning and sequencing of the complementary DNA
AU - Chang, Tschining
AU - Jiang, Yun Jin
AU - Chiou, Shyh Horng
AU - Chang, Wen Chang
PY - 1988/11/10
Y1 - 1988/11/10
N2 - The nucleotide sequences of γ-crystallin cDNAs cloned from the common carp (Cyprinus carpio) have been determined. The amino-acid sequences derived consist of two polypeptides with 177 and 172 amino-acid residues for γ-m1 and γ-m2, respectively. They exhibit unusually high methionine contents: 12.4% for γ-m1 and 14% for γ-m2. Comparison of both fish γ-crystallins with bovine γ-II crystallin reveals that they are similar in structure. The striking features of both fish γ-crystallins are as follows. (1) Both of them retain the 'conserved' residues, i.e., Tyr-6, Glu-7, Gly-13, Ser-34 and their equivalents in other motifs. (2) they possess the second aromatic residue at position 11. Both of these structural features are considered to be the major factors in stabilizing the folded hairpin structure of the protein. (3) The variable residues in the core region of C-terminal domain are almost all sulfur-containing amino acids, i.e., methionine or cysteine. (4) 30% of the surface hydrophobic groups are composed of methionine. The last two unusual features have been found so far only in these two fish γ-crystallins. The high methionine content may make an important contribution to the protein stability of fish γ-crystallins.
AB - The nucleotide sequences of γ-crystallin cDNAs cloned from the common carp (Cyprinus carpio) have been determined. The amino-acid sequences derived consist of two polypeptides with 177 and 172 amino-acid residues for γ-m1 and γ-m2, respectively. They exhibit unusually high methionine contents: 12.4% for γ-m1 and 14% for γ-m2. Comparison of both fish γ-crystallins with bovine γ-II crystallin reveals that they are similar in structure. The striking features of both fish γ-crystallins are as follows. (1) Both of them retain the 'conserved' residues, i.e., Tyr-6, Glu-7, Gly-13, Ser-34 and their equivalents in other motifs. (2) they possess the second aromatic residue at position 11. Both of these structural features are considered to be the major factors in stabilizing the folded hairpin structure of the protein. (3) The variable residues in the core region of C-terminal domain are almost all sulfur-containing amino acids, i.e., methionine or cysteine. (4) 30% of the surface hydrophobic groups are composed of methionine. The last two unusual features have been found so far only in these two fish γ-crystallins. The high methionine content may make an important contribution to the protein stability of fish γ-crystallins.
KW - (C. carpis)
KW - Amino acid sequence
KW - cDNA
KW - DNA sequence
KW - Methionine content
KW - Sequence homology
KW - γ-Crystallin
UR - http://www.scopus.com/inward/record.url?scp=0023796720&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023796720&partnerID=8YFLogxK
U2 - 10.1016/0167-4781(88)90044-9
DO - 10.1016/0167-4781(88)90044-9
M3 - Article
C2 - 3191133
AN - SCOPUS:0023796720
VL - 951
SP - 226
EP - 229
JO - Biochimica et Biophysica Acta - Gene Structure and Expression
JF - Biochimica et Biophysica Acta - Gene Structure and Expression
SN - 0167-4781
IS - 1
ER -