Publikationsdatum:
2001-02-07
Beschreibung:
The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5'-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5'-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawaguchi, K -- Ishiwata, S -- New York, N.Y. -- Science. 2001 Jan 26;291(5504):667-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, School of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11158681" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
Adenosine Diphosphate/*metabolism
;
Adenosine Triphosphate/metabolism
;
Adenylyl Imidodiphosphate/*metabolism
;
Animals
;
Cattle
;
Elasticity
;
Kinesin/*metabolism
;
Kinetics
;
Microtubules/metabolism
;
Models, Biological
;
Swine
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
