Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
32
|
| pubmed:dateCreated |
1997-9-5
|
| pubmed:abstractText |
As a molecular motor, dynein must coordinate ATP hydrolysis with conformational changes that lead to processive interactions with a microtubule and generate force. To understand how these processes occur, we have begun to map functional domains of a dynein heavy chain from Dictyostelium. The carboxyl-terminal 10-kilobase region of the heavy chain encodes a 380-kDa polypeptide that approximates the globular head domain. Attempts to further truncate this region fail to produce polypeptides that either bind microtubules or UV-vanadate cleave, indicating that the entire 10-kilobase fragment is necessary to produce a properly folded functional dynein head. We have further identified a region just downstream from the fourth P-loop that appears to constitute at least part of the microtubule-binding domain (amino acids 3182-3818). When deleted, the resulting head domain polypeptide no longer binds microtubules; when the excised region is expressed in vitro, it cosediments with added tubulin polymer. This microtubule-binding domain falls within an area of the molecule predicted to form extended alpha-helices. At least four discrete sites appear to coordinate activities required to bind the tubulin polymer, indicating that the interaction of dynein with microtubules is complex.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
8
|
| pubmed:volume |
272
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
19714-8
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:9242627-Adenosine Triphosphate,
pubmed-meshheading:9242627-Animals,
pubmed-meshheading:9242627-Binding Sites,
pubmed-meshheading:9242627-Cytoplasm,
pubmed-meshheading:9242627-Dictyostelium,
pubmed-meshheading:9242627-Dyneins,
pubmed-meshheading:9242627-Hydrolysis,
pubmed-meshheading:9242627-Microtubules,
pubmed-meshheading:9242627-Molecular Sequence Data,
pubmed-meshheading:9242627-Open Reading Frames,
pubmed-meshheading:9242627-Protein Binding,
pubmed-meshheading:9242627-Protein Biosynthesis,
pubmed-meshheading:9242627-Protein Conformation,
pubmed-meshheading:9242627-Protein Folding,
pubmed-meshheading:9242627-Sequence Deletion,
pubmed-meshheading:9242627-Transcription, Genetic,
pubmed-meshheading:9242627-Ultraviolet Rays,
pubmed-meshheading:9242627-Vanadates
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Identification of a microtubule-binding domain in a cytoplasmic dynein heavy chain.
|
| pubmed:affiliation |
Division of Molecular Medicine, Wadsworth Center, Empire State Plaza, Albany, New York 12201-0509, USA. Michael.Koonce@wadsworth.org
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|