Identification of an actin-binding protein from Dictyostelium as elongation factor 1a.
Nature
; 347(6292): 494-6, 1990 Oct 04.
Article
in En
| MEDLINE
| ID: mdl-2215665
ABSTRACT
Indirect evidence has implicated an interaction between the cytoskeleton and the protein synthetic machinery. Two recent reports have linked the elongation factor 1a (EF-1a) which is involved in protein synthesis, with the microtubular cytoskeleton. In situ hybridization has, however, revealed that the messages for certain cytoskeletal proteins are preferentially associated with actin filaments. ABP-50 is an abundant actin filament bundling protein of native relative molecular mass 50,000 (50K) isolated from Dictyostelium discoideum. Immunofluorescence studies show that ABP-50 is present in filopodia and other cortical regions that contain actin filament bundles. In addition, ABP-50 binds to monomeric actin in the cytosol of unstimulated cells and the association of ABP-50 with the actin cytoskeleton is regulated during chemotaxis. Through complementary DNA sequencing and subsequent functional analysis, we have identified ABP-50 as D. discoideum EF-1a. The ability of EF-1a to bind reversibly to the actin cytoskeleton upon stimulation could provide a mechanism for spatially and temporally regulated protein synthesis in eukaryotic cells.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptide Elongation Factors
/
Dictyostelium
/
Genes, Fungal
/
Microfilament Proteins
Type of study:
Diagnostic_studies
/
Prognostic_studies
Language:
En
Journal:
Nature
Year:
1990
Document type:
Article