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Neck-Linker Length Dependence of Processive Kinesin-5 Motility.
MedLine Citation:
PMID:  22789568     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Processive motility of individual molecules is essential for the function of many kinesin motors. Processivity for kinesins relies on communication between the two heads of a dimeric molecule, such that binding strictly alternates. The main communicating elements are believed to be the two neck linkers connecting the motors' stalks and heads. A proposed mechanism for coordination is the transmission of stress through the neck linkers. It is believed that the efficiency of gating depends on the length of the neck linker. Recent studies have presented support for a simple model in which the length of the neck linker directly controls the degree of processivity. Based on a previously published Kinesin-1/Kinesin-5 chimera, Eg5Kin, we have analyzed the motility of 12 motor constructs: we have varied the length of the neck linker in the range between 9 and 21 amino acids using the corresponding native Kinesin-5 sequence (Xenopus laevis Eg5). We found, surprisingly, that neither velocity nor force generation depended on neck-linker length. We also found that constructs with short neck linkers, down to 12 amino acids, were still highly processive, while processivity was lost at a length of 9 amino acids. Run lengths were maximal with neck linkers close to the native Kinesin-5 length and decreased beyond that length. This finding generally confirms the coordinating role of the neck linker for kinesin motility, but challenges the simplest model postulating a motor-type independent optimal length. Instead our results suggest that different kinesins might be optimized for different neck-linker lengths.
Authors:
André Düselder; Christina Thiede; Christoph F Schmidt; Stefan Lakämper
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-7-9
Journal Detail:
Title:  Journal of molecular biology     Volume:  -     ISSN:  1089-8638     ISO Abbreviation:  -     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-7-13     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012. Published by Elsevier Ltd.
Affiliation:
Drittes Physikalisches Institut, Georg-August-Universität Göttingen, Germany.
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