Myelin basic protein has multiple calmodulin-binding sites

David S. Libich; Christopher M.D. Hill; Jeffery D. Haines; George Harauz

doi:10.1016/S0006-291X(03)01380-9

Myelin basic protein has multiple calmodulin-binding sites

David S. Libich, Christopher M.D. Hill, Jeffery D. Haines, George Harauz

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

31 Scopus citations

Abstract

Myelin basic protein (MBP) has been shown to bind calmodulin (CaM) in a specific Ca²⁺-dependent manner via a primary target sequence at its C-terminus [Protein Sci. 12 (2003) 1507]. Upon deimination of MBP, the nature of the interaction changed significantly, suggesting either a new binding site or different conformers with different affinities for CaM. In order to resolve this issue, we investigated here the CaM-binding properties of N- and C-terminal deletion mutants of MBP using Trp fluorescence spectroscopy and mass spectrometry. We conclude that there is an additional CaM-binding site on MBP in a central segment (we posit murine residues 82-93) that forms an amphipathic α-helix.

Original language	English (US)
Pages (from-to)	313-319
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	308
Issue number	2
DOIs	https://doi.org/10.1016/S0006-291X(03)01380-9
State	Published - Aug 22 2003
Externally published	Yes

Keywords

Acrylamide quenching
Calmodulin
Fluorescence spectroscopy
Mass spectroscopy
Myelin basic protein

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry
Cell Biology

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10.1016/S0006-291X(03)01380-9

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@article{cbe0acea377a42cea3a53b407496ed23,

title = "Myelin basic protein has multiple calmodulin-binding sites",

abstract = "Myelin basic protein (MBP) has been shown to bind calmodulin (CaM) in a specific Ca2+-dependent manner via a primary target sequence at its C-terminus [Protein Sci. 12 (2003) 1507]. Upon deimination of MBP, the nature of the interaction changed significantly, suggesting either a new binding site or different conformers with different affinities for CaM. In order to resolve this issue, we investigated here the CaM-binding properties of N- and C-terminal deletion mutants of MBP using Trp fluorescence spectroscopy and mass spectrometry. We conclude that there is an additional CaM-binding site on MBP in a central segment (we posit murine residues 82-93) that forms an amphipathic α-helix.",

keywords = "Acrylamide quenching, Calmodulin, Fluorescence spectroscopy, Mass spectroscopy, Myelin basic protein",

author = "Libich, {David S.} and Hill, {Christopher M.D.} and Haines, {Jeffery D.} and George Harauz",

note = "Funding Information: This work was supported by the Canadian Institutes of Health Research, by the Natural Sciences and Engineering Research Council of Canada, and by the Multiple Sclerosis Society of Canada. We are grateful to Dr. Denise Wood, Hospital for Sick Children, Toronto, for arranging the mass spectrometry.",

year = "2003",

month = aug,

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doi = "10.1016/S0006-291X(03)01380-9",

language = "English (US)",

volume = "308",

pages = "313--319",

journal = "Biochemical and Biophysical Research Communications",

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T1 - Myelin basic protein has multiple calmodulin-binding sites

AU - Libich, David S.

AU - Hill, Christopher M.D.

AU - Haines, Jeffery D.

AU - Harauz, George

N1 - Funding Information: This work was supported by the Canadian Institutes of Health Research, by the Natural Sciences and Engineering Research Council of Canada, and by the Multiple Sclerosis Society of Canada. We are grateful to Dr. Denise Wood, Hospital for Sick Children, Toronto, for arranging the mass spectrometry.

PY - 2003/8/22

Y1 - 2003/8/22

N2 - Myelin basic protein (MBP) has been shown to bind calmodulin (CaM) in a specific Ca2+-dependent manner via a primary target sequence at its C-terminus [Protein Sci. 12 (2003) 1507]. Upon deimination of MBP, the nature of the interaction changed significantly, suggesting either a new binding site or different conformers with different affinities for CaM. In order to resolve this issue, we investigated here the CaM-binding properties of N- and C-terminal deletion mutants of MBP using Trp fluorescence spectroscopy and mass spectrometry. We conclude that there is an additional CaM-binding site on MBP in a central segment (we posit murine residues 82-93) that forms an amphipathic α-helix.

AB - Myelin basic protein (MBP) has been shown to bind calmodulin (CaM) in a specific Ca2+-dependent manner via a primary target sequence at its C-terminus [Protein Sci. 12 (2003) 1507]. Upon deimination of MBP, the nature of the interaction changed significantly, suggesting either a new binding site or different conformers with different affinities for CaM. In order to resolve this issue, we investigated here the CaM-binding properties of N- and C-terminal deletion mutants of MBP using Trp fluorescence spectroscopy and mass spectrometry. We conclude that there is an additional CaM-binding site on MBP in a central segment (we posit murine residues 82-93) that forms an amphipathic α-helix.

KW - Acrylamide quenching

KW - Calmodulin

KW - Fluorescence spectroscopy

KW - Mass spectroscopy

KW - Myelin basic protein

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U2 - 10.1016/S0006-291X(03)01380-9

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AN - SCOPUS:0042093636

SN - 0006-291X

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EP - 319

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Myelin basic protein has multiple calmodulin-binding sites

Abstract

Keywords

ASJC Scopus subject areas

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