Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
19
|
| pubmed:dateCreated |
1995-6-15
|
| pubmed:abstractText |
The actin Ser14 hydroxyl is one of a number of ligands that binds to the gamma-phosphate of ATP thereby stabilizing the actin.ATP complex. In yeast actin, conversion of Ser14 to Ala (S14A), causes a temperature-sensitive phenotype in vivo and temperature-sensitive polymerization defects in vitro (Chen, X., and Rubenstein, P. A. (1995) J. Biol. Chem. 270, 11406-11414). Here, using a new luciferase-based procedure, we show that the mutation results in a 40-60-fold decrease in actin's affinity for ATP. The mutation causes a decrease in the intrinsic ATPase activity of both Ca- and Mg-G-actin at 30 degrees C and alters the protease susceptibility of sites on subdomain 2. Ca-S14A-actin but not Mg-S14A-actin binds etheno-ATP at 37 degrees C. Intrinsic tryptophan fluorescence measurements show that at 37 degrees C, Mg-S14A-actin but not the calcium form unfolds. CD measurements show the mutation causes a decrease in the apparent denaturation temperature for Ca-actin from 57 to 45 degrees C and for the magnesium form a decrease from 52 to 40 degrees C. Based on a re-examination of actin's crystal structure coordinates, we propose that the Ser14 hydroxyl forms a polar bridge between the ATP gamma-phosphate and the amide nitrogen of Gly74, thus conferring additional stability on the actin small domain.
|
| 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 Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Serine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
12
|
| pubmed:volume |
270
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
11415-23
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:7744778-Actins,
pubmed-meshheading:7744778-Adenosine Triphosphate,
pubmed-meshheading:7744778-Alanine,
pubmed-meshheading:7744778-Amino Acid Sequence,
pubmed-meshheading:7744778-Animals,
pubmed-meshheading:7744778-Binding Sites,
pubmed-meshheading:7744778-Calcium,
pubmed-meshheading:7744778-Drug Stability,
pubmed-meshheading:7744778-Hot Temperature,
pubmed-meshheading:7744778-Kinetics,
pubmed-meshheading:7744778-Magnesium,
pubmed-meshheading:7744778-Models, Structural,
pubmed-meshheading:7744778-Muscle, Skeletal,
pubmed-meshheading:7744778-Point Mutation,
pubmed-meshheading:7744778-Protein Conformation,
pubmed-meshheading:7744778-Protein Denaturation,
pubmed-meshheading:7744778-Rabbits,
pubmed-meshheading:7744778-Saccharomyces cerevisiae,
pubmed-meshheading:7744778-Serine,
pubmed-meshheading:7744778-Thermodynamics
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
The effect of the S14A mutation on the conformation and thermostability of Saccharomyces cerevisiae G-actin and its interaction with adenine nucleotides.
|
| pubmed:affiliation |
Department of Biochemistry, University of Iowa College of Medicine, Iowa City 52242-1104, USA.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|