Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability

Tong Jin Zhao; Shan Feng; Yong Liang Wang; Yang Liu; Xue Chun Luo; Hai Meng Zhou; Yong Bin Yan

doi:10.1016/j.febslet.2006.05.076

Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability

Tong Jin Zhao, Shan Feng, Yong Liang Wang, Yang Liu, Xue Chun Luo, Hai Meng Zhou, Yong Bin Yan

Molecular Genetics

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

28 Scopus citations

Abstract

Creatine kinase (CK) is a key enzyme in vertebrate excitable tissues. In this research, five conserved residues located on the intra-subunit domain-domain interface were mutated to explore their role in the activity and structural stability of CK. The mutations of Val72 and Gly73 decreased both the activity and stability of CK. The mutations of Cys74 and Val75, which had no significant effect on CK activity and structure, gradually decreased the stability and reactivation of CK. Our results suggested that the mutations might modify the correct positioning of the loop contributing to domain-domain interactions, and result in decreased stability against denaturation.

Original language	English (US)
Pages (from-to)	3835-3840
Number of pages	6
Journal	FEBS Letters
Volume	580
Issue number	16
DOIs	https://doi.org/10.1016/j.febslet.2006.05.076
State	Published - Jul 10 2006

Keywords

Creatine kinase
Domain-domain interactions
Folding intermediate
Phosphagen kinase
Structural stability

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2006.05.076

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title = "Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability",

abstract = "Creatine kinase (CK) is a key enzyme in vertebrate excitable tissues. In this research, five conserved residues located on the intra-subunit domain-domain interface were mutated to explore their role in the activity and structural stability of CK. The mutations of Val72 and Gly73 decreased both the activity and stability of CK. The mutations of Cys74 and Val75, which had no significant effect on CK activity and structure, gradually decreased the stability and reactivation of CK. Our results suggested that the mutations might modify the correct positioning of the loop contributing to domain-domain interactions, and result in decreased stability against denaturation.",

keywords = "Creatine kinase, Domain-domain interactions, Folding intermediate, Phosphagen kinase, Structural stability",

author = "Zhao, {Tong Jin} and Shan Feng and Wang, {Yong Liang} and Yang Liu and Luo, {Xue Chun} and Zhou, {Hai Meng} and Yan, {Yong Bin}",

note = "Funding Information: The authors thank the anonymous reviewers for their helpful suggestions. This investigation was supported by Grants 30500084 (to Y.-B. Yan) and 30221003 (to H.-M. Zhou) from the National Natural Science Foundation of China, Grant 101023 from the Fok Ying Tong Education Foundation (to Y.-B. Yan), and by funds from Jiaxing, Zhejiang (to H.-M. Zhou). ",

year = "2006",

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doi = "10.1016/j.febslet.2006.05.076",

language = "English (US)",

volume = "580",

pages = "3835--3840",

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T1 - Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability

AU - Zhao, Tong Jin

AU - Feng, Shan

AU - Wang, Yong Liang

AU - Liu, Yang

AU - Luo, Xue Chun

AU - Zhou, Hai Meng

AU - Yan, Yong Bin

N1 - Funding Information: The authors thank the anonymous reviewers for their helpful suggestions. This investigation was supported by Grants 30500084 (to Y.-B. Yan) and 30221003 (to H.-M. Zhou) from the National Natural Science Foundation of China, Grant 101023 from the Fok Ying Tong Education Foundation (to Y.-B. Yan), and by funds from Jiaxing, Zhejiang (to H.-M. Zhou).

PY - 2006/7/10

Y1 - 2006/7/10

N2 - Creatine kinase (CK) is a key enzyme in vertebrate excitable tissues. In this research, five conserved residues located on the intra-subunit domain-domain interface were mutated to explore their role in the activity and structural stability of CK. The mutations of Val72 and Gly73 decreased both the activity and stability of CK. The mutations of Cys74 and Val75, which had no significant effect on CK activity and structure, gradually decreased the stability and reactivation of CK. Our results suggested that the mutations might modify the correct positioning of the loop contributing to domain-domain interactions, and result in decreased stability against denaturation.

AB - Creatine kinase (CK) is a key enzyme in vertebrate excitable tissues. In this research, five conserved residues located on the intra-subunit domain-domain interface were mutated to explore their role in the activity and structural stability of CK. The mutations of Val72 and Gly73 decreased both the activity and stability of CK. The mutations of Cys74 and Val75, which had no significant effect on CK activity and structure, gradually decreased the stability and reactivation of CK. Our results suggested that the mutations might modify the correct positioning of the loop contributing to domain-domain interactions, and result in decreased stability against denaturation.

KW - Creatine kinase

KW - Domain-domain interactions

KW - Folding intermediate

KW - Phosphagen kinase

KW - Structural stability

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SP - 3835

EP - 3840

JO - FEBS Letters

JF - FEBS Letters

IS - 16

ER -

Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability

Abstract

Keywords

ASJC Scopus subject areas

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