Ontology highlight
ABSTRACT:
SUBMITTER: Pittman YR
PROVIDER: S-EPMC2640982 | biostudies-literature | 2009 Feb
REPOSITORIES: biostudies-literature
Pittman Yvette R YR Kandl Kimberly K Lewis Marcus M Valente Louis L Kinzy Terri Goss TG
The Journal of biological chemistry 20081218 7
Eukaryotic translation elongation factor 1A (eEF1A) both shuttles aminoacyl-tRNA (aa-tRNA) to the ribosome and binds and bundles actin. A single domain of eEF1A is proposed to bind actin, aa-tRNA and the guanine nucleotide exchange factor eEF1Balpha. We show that eEF1Balpha has the ability to disrupt eEF1A-induced actin organization. Mutational analysis of eEF1Balpha F163, which binds in this domain, demonstrates effects on growth, eEF1A binding, nucleotide exchange activity, and cell morphology ...[more]