Source:http://linkedlifedata.com/resource/pubmed/id/19059909
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
2009-2-2
|
pubmed:abstractText |
The mammalian class IX myosin Myo9b can move considerable distances along actin filaments before it dissociates. This is remarkable, because it is single headed and because the rate-limiting step in its ATPase cycle is ATP hydrolysis. Thus, it spends most of its cycling time in the ATP-bound state that has a weak affinity for F-actin in other myosins. It has been speculated that the very extended loop 2 in the Myo9b head domain comprises an additional actin-binding site that prevents it from dissociation in the weak binding states. Here we show that two regions in the loop 2 determine the F-actin concentrations needed to maximally activate the steady-state ATPase activity. Together these two regions regulate the amount capable of binding F-actin and the affinity of the nucleotide-free state. The isolated loop 2 behaved like an entropic spring and bound stoichiometrically and with high affinity to F-actin. Subfragment 1 from skeletal muscle myosin II bound to F-actin simultaneously with the isolated loop 2 of Myo9b and could not displace it. Furthermore, the present results imply also a regulatory role for the tail region. Taken together, the results demonstrate that the extended loop 2 in Myo9b binds F-actin and influences the binding of the conventional stereo-specific actin-binding site.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
6
|
pubmed:volume |
284
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3663-71
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:19059909-Actins,
pubmed-meshheading:19059909-Adenosine Triphosphate,
pubmed-meshheading:19059909-Animals,
pubmed-meshheading:19059909-Binding Sites,
pubmed-meshheading:19059909-Cell Line,
pubmed-meshheading:19059909-Hydrolysis,
pubmed-meshheading:19059909-Myosins,
pubmed-meshheading:19059909-Protein Binding,
pubmed-meshheading:19059909-Protein Structure, Secondary,
pubmed-meshheading:19059909-Protein Structure, Tertiary,
pubmed-meshheading:19059909-Rats
|
pubmed:year |
2009
|
pubmed:articleTitle |
Functional role of the extended loop 2 in the myosin 9b head for binding F-actin.
|
pubmed:affiliation |
Institute of General Zoology and Genetics, Westfalian Wilhelms-University Münster, Münster 48149, Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|