Source:http://linkedlifedata.com/resource/pubmed/id/11844798
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
18
|
| pubmed:dateCreated |
2002-4-29
|
| pubmed:abstractText |
Profilin and beta/gamma-actin from calf thymus were covalently linked using the zero-length cross-linker 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide in combination with N-hydroxysuccinimide, yielding a single product with an apparent molecular mass of 60 kDa. Sequence analysis and x-ray crystallographic investigations showed that the cross-linked residues were glutamic acid 82 of profilin and lysine 113 of actin. The cross-linked complex was shown to bind with high affinity to deoxyribonuclease I and poly(l-proline). It also bound and exchanged ATP with kinetics close to that of unmodified profilin-actin and inhibited the intrinsic ATPase activity of actin. This inhibition occurred even in conditions where actin normally forms filaments. By these criteria the cross-linked profilin-actin complex retains the characteristics of unmodified profilin-actin. However, the cross-linked complex did not form filaments nor copolymerized with unmodified actin, but did interfere with elongation of actin filaments in a concentration-dependent manner. These results support a polymerization mechanism where the profilin-actin heterodimer binds to the (+)-end of actin filaments, followed by dissociation of profilin, and ATP hydrolysis and P(i) release from the actin subunit as it assumes its stable conformation in the helical filament.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Contractile Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Profilins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
3
|
| pubmed:volume |
277
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
15828-33
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:11844798-Actins,
pubmed-meshheading:11844798-Adenosine Triphosphatases,
pubmed-meshheading:11844798-Adenosine Triphosphate,
pubmed-meshheading:11844798-Amino Acid Sequence,
pubmed-meshheading:11844798-Animals,
pubmed-meshheading:11844798-Binding Sites,
pubmed-meshheading:11844798-Cattle,
pubmed-meshheading:11844798-Contractile Proteins,
pubmed-meshheading:11844798-Cross-Linking Reagents,
pubmed-meshheading:11844798-Crystallization,
pubmed-meshheading:11844798-Dimerization,
pubmed-meshheading:11844798-Kinetics,
pubmed-meshheading:11844798-Microfilament Proteins,
pubmed-meshheading:11844798-Microscopy, Electron,
pubmed-meshheading:11844798-Models, Molecular,
pubmed-meshheading:11844798-Profilins,
pubmed-meshheading:11844798-Protein Isoforms,
pubmed-meshheading:11844798-Protein Multimerization,
pubmed-meshheading:11844798-Thymus Gland
|
| pubmed:year |
2002
|
| pubmed:articleTitle |
A cross-linked profilin-actin heterodimer interferes with elongation at the fast-growing end of F-actin.
|
| pubmed:affiliation |
Department of Cell Biology, the Wenner-Gren Institute, Stockholm University, S-106 91 Stockholm, Sweden.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|