Casein kinase-2 phosphorylates serine-2 in the β-subunit of initiation factor-2

Stephanie J. Clark; Anthony J. Ashford; Nigel T. Price; Christopher G. Proud

doi:10.1016/0167-4889(89)90065-7

Casein kinase-2 phosphorylates serine-2 in the β-subunit of initiation factor-2

Stephanie J. Clark, Anthony J. Ashford, Nigel T. Price, Christopher G. Proud

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

Abstract

We have previously presented evidence which suggests that casein kinase-2 phosphorylates a serine residue near the N-terminus of the β-subunit of the initiation factor eIF-2 (Clark, S.J. et al. Biochim. Biophys. Acta 968, 211-219). We now report further data which confirm that it is serine-2 which is phosphorylated by casein kinase-2. This data includes (1) the electrophoretic mobilities of the phosphopeptides produced by different cleavage techniques, (2) the amino acid composition of the principal phosphopeptide generated by treatment with cyanogen bromide and (3) the resistance of this phosphopeptide to Edman degradation.

Original language	English
Pages (from-to)	377-380
Number of pages	4
Journal	BBA - Molecular Cell Research
Volume	1010
Issue number	3
DOIs	https://doi.org/10.1016/0167-4889(89)90065-7
Publication status	Published or Issued - 6 Mar 1989
Externally published	Yes

Keywords

Casein kinase-2
Initiation factor
Protein phosphorylation
Protein synthesis

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/0167-4889(89)90065-7

Cite this

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title = "Casein kinase-2 phosphorylates serine-2 in the β-subunit of initiation factor-2",

abstract = "We have previously presented evidence which suggests that casein kinase-2 phosphorylates a serine residue near the N-terminus of the β-subunit of the initiation factor eIF-2 (Clark, S.J. et al. Biochim. Biophys. Acta 968, 211-219). We now report further data which confirm that it is serine-2 which is phosphorylated by casein kinase-2. This data includes (1) the electrophoretic mobilities of the phosphopeptides produced by different cleavage techniques, (2) the amino acid composition of the principal phosphopeptide generated by treatment with cyanogen bromide and (3) the resistance of this phosphopeptide to Edman degradation.",

keywords = "Casein kinase-2, Initiation factor, Protein phosphorylation, Protein synthesis",

author = "Clark, {Stephanie J.} and Ashford, {Anthony J.} and Price, {Nigel T.} and Proud, {Christopher G.}",

note = "Funding Information: We are very grateful to Dr. John Hershey and his colleagues at the University of California (Davis) for allowing us to quote their data on the sequence of eIF-2/~ prior to full publication. We wish to thank David Colthurst for his excellent assistance and in particular for preparing the casein kinase-2 used in this work, and Dr. David Campbell (University of ~'undee) for performing the amino acid analysis. This work was supported by a grant (to C.G.P.) from the Science and Engineering Research Council, U.K.",

year = "1989",

month = mar,

day = "6",

doi = "10.1016/0167-4889(89)90065-7",

language = "English",

volume = "1010",

pages = "377--380",

journal = "Biochimica et Biophysica Acta - Molecular Cell Research",

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publisher = "Elsevier",

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TY - JOUR

T1 - Casein kinase-2 phosphorylates serine-2 in the β-subunit of initiation factor-2

AU - Clark, Stephanie J.

AU - Ashford, Anthony J.

AU - Price, Nigel T.

AU - Proud, Christopher G.

N1 - Funding Information: We are very grateful to Dr. John Hershey and his colleagues at the University of California (Davis) for allowing us to quote their data on the sequence of eIF-2/~ prior to full publication. We wish to thank David Colthurst for his excellent assistance and in particular for preparing the casein kinase-2 used in this work, and Dr. David Campbell (University of ~'undee) for performing the amino acid analysis. This work was supported by a grant (to C.G.P.) from the Science and Engineering Research Council, U.K.

PY - 1989/3/6

Y1 - 1989/3/6

N2 - We have previously presented evidence which suggests that casein kinase-2 phosphorylates a serine residue near the N-terminus of the β-subunit of the initiation factor eIF-2 (Clark, S.J. et al. Biochim. Biophys. Acta 968, 211-219). We now report further data which confirm that it is serine-2 which is phosphorylated by casein kinase-2. This data includes (1) the electrophoretic mobilities of the phosphopeptides produced by different cleavage techniques, (2) the amino acid composition of the principal phosphopeptide generated by treatment with cyanogen bromide and (3) the resistance of this phosphopeptide to Edman degradation.

AB - We have previously presented evidence which suggests that casein kinase-2 phosphorylates a serine residue near the N-terminus of the β-subunit of the initiation factor eIF-2 (Clark, S.J. et al. Biochim. Biophys. Acta 968, 211-219). We now report further data which confirm that it is serine-2 which is phosphorylated by casein kinase-2. This data includes (1) the electrophoretic mobilities of the phosphopeptides produced by different cleavage techniques, (2) the amino acid composition of the principal phosphopeptide generated by treatment with cyanogen bromide and (3) the resistance of this phosphopeptide to Edman degradation.

KW - Casein kinase-2

KW - Initiation factor

KW - Protein phosphorylation

KW - Protein synthesis

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U2 - 10.1016/0167-4889(89)90065-7

DO - 10.1016/0167-4889(89)90065-7

M3 - Article

C2 - 2493264

AN - SCOPUS:0024592441

VL - 1010

SP - 377

EP - 380

JO - Biochimica et Biophysica Acta - Molecular Cell Research

JF - Biochimica et Biophysica Acta - Molecular Cell Research

SN - 0167-4889

IS - 3

ER -

Casein kinase-2 phosphorylates serine-2 in the β-subunit of initiation factor-2

Abstract

Keywords

ASJC Scopus subject areas

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