THE STRUCTURE OF PROTEIN PHOSPHATASE-2A IS AS HIGHLY CONSERVED AS THAT OF PROTEIN PHOSPHATASE-1

被引：65

作者：

ORGAD, S

BREWIS, ND

ALPHEY, L

AXTON, JM

DUDAI, Y

COHEN, PTW

机构：

[1] UNIV DUNDEE,INST MED SCI,DEPT BIOCHEM,MRC,PROT PHOSPHORYLAT UNIT,DUNDEE DD1 4HN,SCOTLAND

[2] WEIZMANN INST SCI,DEPT NEUROBIOL,IL-76100 REHOVOT,ISRAEL

[3] UNIV DUNDEE,DEPT BIOCHEM,CANC RES CAMPAIGN CELL CYCLE GENET GRD,DUNDEE DD1 4HN,SCOTLAND

来源：

FEBS LETTERS | 1990年 / 275卷 / 1-2期

关键词：

Amino acid sequence; cDNA cloning; Drosophila melanogaster; Nucleotide sequence; Protein phosphatase; Sequence homology;

D O I：

10.1016/0014-5793(90)81435-Q

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

cDNA coding for protein phosphatase 2A (PP2A) has been isolated from Drosophila head and eye imaginal disc libraries. Drosophila PP2A mRNA is expressed throughout development, but is most abundant in the early embryo. The cDNA hybridises to a single site on the left area of the second chromosomes at position 28D2-4. The deduced amino acid sequence (309 residues) of Drosophila PP2A shows 94% identity with either rabbit PP2Aα or PP2Aβ, indicating that PP2A maybe the most conserved of all known enzymes. © 1990.

引用

页码：44 / 48

页数：5

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[1] IS CONTIGUITY DETECTION IN CLASSICAL-CONDITIONING A SYSTEM OR A CELLULAR PROPERTY - LEARNING IN APLYSIA SUGGESTS A POSSIBLE MOLECULAR SITE [J].