Deletion analysis of the dystrophin-actin binding domain

K. Corrado; P. L. Mills; J. S. Chamberlain

doi:10.1016/0014-5793(94)00397-1

Deletion analysis of the dystrophin-actin binding domain

K. Corrado, P. L. Mills, J. S. Chamberlain

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

97 Scopus citations

Abstract

Three sequence motifs at the N-terminus of dystrophin have previously been proposed to be important for binding to actin. By analyzing a series of purified bacterial fusion proteins deleted for each of these sites we have demonstrated that none of the three are critical for dystrophin-actin interactions. Instead, our data suggest that sequences in the N-terminal 90 amino acids of dystrophin, excluding a conserved KTFT motif, contain the major site for interaction with actin.

Original language	English (US)
Pages (from-to)	255-260
Number of pages	6
Journal	FEBS Letters
Volume	344
Issue number	2-3
DOIs	https://doi.org/10.1016/0014-5793(94)00397-1
State	Published - May 16 1994
Externally published	Yes

Keywords

Actin binding site
Duchenne muscular dystrophy
Dystrophin
α-Actinin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(94)00397-1

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title = "Deletion analysis of the dystrophin-actin binding domain",

abstract = "Three sequence motifs at the N-terminus of dystrophin have previously been proposed to be important for binding to actin. By analyzing a series of purified bacterial fusion proteins deleted for each of these sites we have demonstrated that none of the three are critical for dystrophin-actin interactions. Instead, our data suggest that sequences in the N-terminal 90 amino acids of dystrophin, excluding a conserved KTFT motif, contain the major site for interaction with actin.",

keywords = "Actin binding site, Duchenne muscular dystrophy, Dystrophin, α-Actinin",

author = "K. Corrado and Mills, {P. L.} and Chamberlain, {J. S.}",

note = "Funding Information: AcknowledgementsW: e thank the members of the Chamberlain Laboratory for thoughtful discussions, Greg Cox for providing the C-DYS plasmid, and Drs. Brian Haarer, Susan Brown and Kuan Wang for helpful advice and suggestions. We also thank the University of Michigan Multipurpose Arthritis and Musculoskeletal Disease Center Core Laboratories for oligonucleotide and peptide synthesis (supported by Grant NIH P60AR20557). This work was supported by a grant from the Muscular Dystrophy Association and by Grant NIH ROlAR40864 (to J.S.C.). K.C. was supported by a postdoctoral fellowship from the Muscular Dystrophy Association.",

year = "1994",

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doi = "10.1016/0014-5793(94)00397-1",

language = "English (US)",

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pages = "255--260",

journal = "FEBS Letters",

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AU - Corrado, K.

AU - Mills, P. L.

AU - Chamberlain, J. S.

N1 - Funding Information: AcknowledgementsW: e thank the members of the Chamberlain Laboratory for thoughtful discussions, Greg Cox for providing the C-DYS plasmid, and Drs. Brian Haarer, Susan Brown and Kuan Wang for helpful advice and suggestions. We also thank the University of Michigan Multipurpose Arthritis and Musculoskeletal Disease Center Core Laboratories for oligonucleotide and peptide synthesis (supported by Grant NIH P60AR20557). This work was supported by a grant from the Muscular Dystrophy Association and by Grant NIH ROlAR40864 (to J.S.C.). K.C. was supported by a postdoctoral fellowship from the Muscular Dystrophy Association.

PY - 1994/5/16

Y1 - 1994/5/16

N2 - Three sequence motifs at the N-terminus of dystrophin have previously been proposed to be important for binding to actin. By analyzing a series of purified bacterial fusion proteins deleted for each of these sites we have demonstrated that none of the three are critical for dystrophin-actin interactions. Instead, our data suggest that sequences in the N-terminal 90 amino acids of dystrophin, excluding a conserved KTFT motif, contain the major site for interaction with actin.

AB - Three sequence motifs at the N-terminus of dystrophin have previously been proposed to be important for binding to actin. By analyzing a series of purified bacterial fusion proteins deleted for each of these sites we have demonstrated that none of the three are critical for dystrophin-actin interactions. Instead, our data suggest that sequences in the N-terminal 90 amino acids of dystrophin, excluding a conserved KTFT motif, contain the major site for interaction with actin.

KW - Actin binding site

KW - Duchenne muscular dystrophy

KW - Dystrophin

KW - α-Actinin

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Deletion analysis of the dystrophin-actin binding domain

Abstract

Keywords

ASJC Scopus subject areas

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