| http://purl.uniprot.org/citations/16118223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16118223 | http://www.w3.org/2000/01/rdf-schema#comment | "To determine the reason for the inviability of Saccharomyces cerevisiae with skeletal muscle actin, we introduced into yeast actin the first variant muscle residue from the C-terminal end, H372R. Arg is also found at this position in non-yeast nonmuscle actins. The substitution caused retarded growth on glucose and an inability to use glycerol as a sole carbon source. The mitochondria were clumped and had lost their DNA, the vacuole appeared hypervesiculated, and the actin cytoskeleton became somewhat depolarized. Introduction of the second muscle actin-specific substitution, S365A, rescued these defects. Suppression was also achieved by introducing the four acidic N-terminal residues of muscle actin in place of the two found in yeast actin. The H372R substitution results in an increase in polymerization-dependent fluorescence of Cys-374 pyrene-labeled actin. H372R actin polymerizes slightly faster than wild-type (WT) actin. Yeast actin-related proteins 2 and 3 (Arp2/3) accelerates the polymerization of H372R actin to a much greater extent than WT actin. The two suppressors did not affect the rate of H372R actin polymerization in the absence of an Arp2/3 complex. In contrast, the S365A substitution dampened the rate of Arp2/3 complex-stimulated H372R actin polymerization, and the addition of the four acidic N-terminal residues caused this rate to decrease below that observed with WT actin in the presence of Arp2/3. Structural analysis of the mutations suggests the presence of stringent steric and ionic requirements for the bottom of actin subdomain 1 and also suggests that there is allosteric communication through subdomain 1 within the actin monomer between the N and C termini."xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m506970200"xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/author | "Rubenstein P.A."xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/author | "Boldogh I.R."xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/author | "Pon L.A."xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/author | "Wen K.K."xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/author | "McKane M."xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/author | "Ramcharan S."xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/pages | "36494-36501"xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/title | "A mammalian actin substitution in yeast actin (H372R) causes a suppressible mitochondria/vacuole phenotype."xsd:string |
| http://purl.uniprot.org/citations/16118223 | http://purl.uniprot.org/core/volume | "280"xsd:string |
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