A novel 27 16 kDa form of subtilisin cleaved actin: structural and functional consequences of cleavage between Ser234 and Ser235

Arash Vahdat; Carl Miller; Martin Phillips; Andras Muhlrad; Emil Reisler

doi:10.1016/0014-5793(95)00446-G

A novel 27 16 kDa form of subtilisin cleaved actin: structural and functional consequences of cleavage between Ser²³⁴ and Ser²³⁵

Arash Vahdat
, Carl Miller
, Martin Phillips
, Andras Muhlrad
, Emil Reisler^*

^*Corresponding author for this work

Institute of Biomedical Research at the Faculty of Dental Medicine

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

11 Scopus citations

Abstract

A new 27/16 kDa form of cleaved actin was prepared by subtilisin cleavage between Ser²³⁴ and Ser²³⁵ of F(MgADP)-actin complexed with BeF_x. The cleavage had little effect on actin-actin interactions as probed in polymerization measurements and by electron microscopy. In circular dichroism melting experiments the thermostability of F-actin was reduced by about 10°C by this cleavage. The in vitro motility and V_max, but not K_m, of actomyosin ATPase were decreased by about 20% upon 27/16 kDa cleavage of F-actin. The binding of tropomyosin to actin was unchanged by this modification.

Original language	English
Pages (from-to)	149-151
Number of pages	3
Journal	FEBS Letters
Volume	365
Issue number	2-3
DOIs	https://doi.org/10.1016/0014-5793(95)00446-G
State	Published - 29 May 1995

Keywords

Actin
Actomyosin interaction
Proteolysis
Structure-function relationship

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10.1016/0014-5793(95)00446-G

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title = "A novel 27 16 kDa form of subtilisin cleaved actin: structural and functional consequences of cleavage between Ser234 and Ser235",

abstract = "A new 27/16 kDa form of cleaved actin was prepared by subtilisin cleavage between Ser234 and Ser235 of F(MgADP)-actin complexed with BeFx. The cleavage had little effect on actin-actin interactions as probed in polymerization measurements and by electron microscopy. In circular dichroism melting experiments the thermostability of F-actin was reduced by about 10°C by this cleavage. The in vitro motility and Vmax, but not Km, of actomyosin ATPase were decreased by about 20\% upon 27/16 kDa cleavage of F-actin. The binding of tropomyosin to actin was unchanged by this modification.",

keywords = "Actin, Actomyosin interaction, Proteolysis, Structure-function relationship",

author = "Arash Vahdat and Carl Miller and Martin Phillips and Andras Muhlrad and Emil Reisler",

year = "1995",

month = may,

day = "29",

doi = "10.1016/0014-5793(95)00446-G",

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T2 - structural and functional consequences of cleavage between Ser234 and Ser235

AU - Vahdat, Arash

AU - Miller, Carl

AU - Phillips, Martin

AU - Muhlrad, Andras

AU - Reisler, Emil

PY - 1995/5/29

Y1 - 1995/5/29

N2 - A new 27/16 kDa form of cleaved actin was prepared by subtilisin cleavage between Ser234 and Ser235 of F(MgADP)-actin complexed with BeFx. The cleavage had little effect on actin-actin interactions as probed in polymerization measurements and by electron microscopy. In circular dichroism melting experiments the thermostability of F-actin was reduced by about 10°C by this cleavage. The in vitro motility and Vmax, but not Km, of actomyosin ATPase were decreased by about 20% upon 27/16 kDa cleavage of F-actin. The binding of tropomyosin to actin was unchanged by this modification.

AB - A new 27/16 kDa form of cleaved actin was prepared by subtilisin cleavage between Ser234 and Ser235 of F(MgADP)-actin complexed with BeFx. The cleavage had little effect on actin-actin interactions as probed in polymerization measurements and by electron microscopy. In circular dichroism melting experiments the thermostability of F-actin was reduced by about 10°C by this cleavage. The in vitro motility and Vmax, but not Km, of actomyosin ATPase were decreased by about 20% upon 27/16 kDa cleavage of F-actin. The binding of tropomyosin to actin was unchanged by this modification.

KW - Actin

KW - Actomyosin interaction

KW - Proteolysis

KW - Structure-function relationship

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JF - FEBS Letters

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ER -

A novel 27 16 kDa form of subtilisin cleaved actin: structural and functional consequences of cleavage between Ser²³⁴ and Ser²³⁵

Abstract

Keywords

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