Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes

Nigel T. Price; Nicholas T. Redpath; Konstantin V. Severinov; David G. Campbell; J. M. Russell; Christopher G. Proud

doi:10.1016/0014-5793(91)80489-P

Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes

Nigel T. Price, Nicholas T. Redpath, Konstantin V. Severinov, David G. Campbell, J. M. Russell, Christopher G. Proud

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

103 Citations (Scopus)

Abstract

The sites in eukaryotic elongation factor eEF-2 phosphorylated by the Ca²⁺/calmodulin-dependent eEF-2 kinase in vitro have been identified. The kinase catalysed the rapid incorporation of one mol of phosphate per mol eEF-2 and the slower incorporation of a second mol. All the phosphorylation sites in eEF-2 are contained in the CNBr fragment corresponding to residues 22-155. Tryptic digestion of phosphorylated eEF-2 yielded 3 phosphopeptides, one being unique to monophosphorylated eEF-2. The phosphorylation sites were identified as threonine residues 56 and 58, the former being more rapidly phosphorylated. Ala-Gly-Glu-Thr-Phe-Thr¹⁴-Asp-Thr¹⁸-Arg. The same sites are labelled in eEF-2 isolated from reticulocyte lysates.

Original language	English
Pages (from-to)	253-258
Number of pages	6
Journal	FEBS Letters
Volume	282
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(91)80489-P
Publication status	Published or Issued - 6 May 1991
Externally published	Yes

Keywords

Calcium/calmodulin
Elongation factor-2
Protein kinase
Protein phosphorylation
Protein synthesis
Rabbit reticulocyte

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(91)80489-P

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@article{83137750f14b457ab38df96e0b90111b,

title = "Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes",

abstract = "The sites in eukaryotic elongation factor eEF-2 phosphorylated by the Ca2+/calmodulin-dependent eEF-2 kinase in vitro have been identified. The kinase catalysed the rapid incorporation of one mol of phosphate per mol eEF-2 and the slower incorporation of a second mol. All the phosphorylation sites in eEF-2 are contained in the CNBr fragment corresponding to residues 22-155. Tryptic digestion of phosphorylated eEF-2 yielded 3 phosphopeptides, one being unique to monophosphorylated eEF-2. The phosphorylation sites were identified as threonine residues 56 and 58, the former being more rapidly phosphorylated. Ala-Gly-Glu-Thr-Phe-Thr14-Asp-Thr18-Arg. The same sites are labelled in eEF-2 isolated from reticulocyte lysates.",

keywords = "Calcium/calmodulin, Elongation factor-2, Protein kinase, Protein phosphorylation, Protein synthesis, Rabbit reticulocyte",

author = "Price, \{Nigel T.\} and Redpath, \{Nicholas T.\} and Severinov, \{Konstantin V.\} and Campbell, \{David G.\} and Russell, \{J. M.\} and Proud, \{Christopher G.\}",

note = "Funding Information: Aeknawledgemema: We arc I\textasciitilde{}rateful to Professor Philip Cohen for allo\textasciitilde{}lnll us to us\textasciitilde{} the flus.phase sequencin8 and. ancillary facilities in tire Department of BiochemlJtry, University of Dundee, This work was supported by =rants from the Science and Enilincerin8 Research Council and the Medical Research Council to CGP, K,S, was the recipient of a Scholarship from the British Council, and performed this work durint\textasciitilde{} this visit to Bristol, We are grateful to Dr, G.R. Drapeau (Montreal) for Asp.N proteinase, and to GsW Rutter (Bristol) \textasciitilde{}or calntodulin,",

year = "1991",

month = may,

day = "6",

doi = "10.1016/0014-5793(91)80489-P",

language = "English",

volume = "282",

pages = "253--258",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "2",

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TY - JOUR

T1 - Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes

AU - Price, Nigel T.

AU - Redpath, Nicholas T.

AU - Severinov, Konstantin V.

AU - Campbell, David G.

AU - Russell, J. M.

AU - Proud, Christopher G.

N1 - Funding Information: Aeknawledgemema: We arc I~rateful to Professor Philip Cohen for allo~lnll us to us~ the flus.phase sequencin8 and. ancillary facilities in tire Department of BiochemlJtry, University of Dundee, This work was supported by =rants from the Science and Enilincerin8 Research Council and the Medical Research Council to CGP, K,S, was the recipient of a Scholarship from the British Council, and performed this work durint~ this visit to Bristol, We are grateful to Dr, G.R. Drapeau (Montreal) for Asp.N proteinase, and to GsW Rutter (Bristol) ~or calntodulin,

PY - 1991/5/6

Y1 - 1991/5/6

N2 - The sites in eukaryotic elongation factor eEF-2 phosphorylated by the Ca2+/calmodulin-dependent eEF-2 kinase in vitro have been identified. The kinase catalysed the rapid incorporation of one mol of phosphate per mol eEF-2 and the slower incorporation of a second mol. All the phosphorylation sites in eEF-2 are contained in the CNBr fragment corresponding to residues 22-155. Tryptic digestion of phosphorylated eEF-2 yielded 3 phosphopeptides, one being unique to monophosphorylated eEF-2. The phosphorylation sites were identified as threonine residues 56 and 58, the former being more rapidly phosphorylated. Ala-Gly-Glu-Thr-Phe-Thr14-Asp-Thr18-Arg. The same sites are labelled in eEF-2 isolated from reticulocyte lysates.

AB - The sites in eukaryotic elongation factor eEF-2 phosphorylated by the Ca2+/calmodulin-dependent eEF-2 kinase in vitro have been identified. The kinase catalysed the rapid incorporation of one mol of phosphate per mol eEF-2 and the slower incorporation of a second mol. All the phosphorylation sites in eEF-2 are contained in the CNBr fragment corresponding to residues 22-155. Tryptic digestion of phosphorylated eEF-2 yielded 3 phosphopeptides, one being unique to monophosphorylated eEF-2. The phosphorylation sites were identified as threonine residues 56 and 58, the former being more rapidly phosphorylated. Ala-Gly-Glu-Thr-Phe-Thr14-Asp-Thr18-Arg. The same sites are labelled in eEF-2 isolated from reticulocyte lysates.

KW - Calcium/calmodulin

KW - Elongation factor-2

KW - Protein kinase

KW - Protein phosphorylation

KW - Protein synthesis

KW - Rabbit reticulocyte

UR - https://www.scopus.com/pages/publications/0025868969

U2 - 10.1016/0014-5793(91)80489-P

DO - 10.1016/0014-5793(91)80489-P

M3 - Article

C2 - 2037042

AN - SCOPUS:0025868969

SN - 0014-5793

VL - 282

SP - 253

EP - 258

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes

Abstract

Keywords

ASJC Scopus subject areas

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