English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Dictyostelium discoideum myosin II: Characterization of functional myosin motor fragments

Kurzawa, S. E., Manstein, D. J., & Geeves, M. A. (1997). Dictyostelium discoideum myosin II: Characterization of functional myosin motor fragments. Biochemistry, 36(2), 317-323. doi:10.1021/bi962166b.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Dictyostelium discoideum myosin II: Characterization of functional myosin motor fragments

Files

show Files
hide Files
:
Biochem_36_1997_317.pdf (Any fulltext), 172KB
 
File Permalink:
-
Name:
Biochem_36_1997_317.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Locator:
http://dx.doi.org/10.1021/bi962166b (Any fulltext)
Description:
-

Creators

show
hide
 Creators:
Kurzawa, S. E., Author
Manstein, Dietmar J.1, Author              
Geeves, Michael A., Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 Abstract: The transient kinetic properties of the recombinant myosin head fragments M761 and M781, which both lack the light chain binding domain (LCBD) and correspond to the first 761 and 781 residues of Dictyostelium discoideum myosin II, were compared with those of the subfragment 1-like fragment M864 and a shorter catalytic domain fragment M754. The properties of M761, M781, and M864 are almost identical in regard to nucleotide binding, nucleotide hydrolysis, actin binding, and the interactions between actin and nucleotide binding sites. Only the rate of the hydrolysis step was significantly faster for M761 and the affinity of M781 for actin significantly weaker than for M864. This indicates that the LCBD plays no major role in the biochemical behavior of the myosin head. In contrast, loss of the peptide between 754 and 761 produced several major changes in the property of M754 as documented previously [Woodward, S. K. A., Geeves, M. A., & Manstein, D. J. (1995) Biochemistry 34, 16056−16064]. We further show that C-terminal extension of M761 with one or two α-actinin repeats has very little effect on the behavior of the protein. The recombinant nature of M761 and the fact that it can be produced and purified in large amounts make it an ideal construct for systematic studies of the structure, kinetics, and function of the myosin motor

Details

show
hide
Language(s): eng - English
 Dates: 1996-11-041996-08-271996-11-041997-01-14
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 36 (2) Sequence Number: - Start / End Page: 317 - 323 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103