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PMID: 2668299 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The Dictyostelium gelation factor shares a putative actin binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation.

The Journal of cell biology ·Vol. 109 ·No. 2 ·1989-08-00 ·Pages 607-18

Noegel AA, Rapp S, Lottspeich F, Schleicher M, Stewart M

Abstract

The 120-kD gelation factor and alpha-actinin are among the most abundant F-actin cross-linking proteins in Dictyostelium discoideum. Both molecules are homodimers and have extended rod-like configurations that are respectively approximately 35 and 40 nm long. Here we report the complete cDNA sequence of the 120-kD gelation factor which codes for a protein of 857 amino acids. Its calculated molecular mass is 92.2 kD which is considerably smaller than suggested by its mobility in SDS-PAGE. Analysis of the sequence shows a region that is highly homologous to D. discoideum alpha-actinin, chicken fibroblast alpha-actinin, and human dystrophin. This conserved domain probably represents an actin binding site that is connected to the rod-forming part of the molecule via a highly charged stretch of amino acids. Whereas the sequence of alpha-actinin (Noegel, A., W. Witke, and M. Schleicher. 1987. FEBS [Fed. Eur. Biochem. Soc.] Lett. 221:391-396) suggests that the extended rod domain of the molecule is based on four spectrin-like repeats with high alpha-helix potential, the rod domain of the 120-kD gelation factor is constructed from six 100-residue repeats that have a high content of glycine and proline residues and which, in contrast to alpha-actinin, do not appear to have a high alpha-helical content. These repeats show a distinctive pattern of regions that have high beta-sheet potential alternating with short zones rich in residues with a high potential for turns. This observation suggests that each 100-residue motif has a cross-beta conformation with approximately nine sheets arranged perpendicular to the long axis of the molecule. In the high beta-potential zones every second residue is often hydrophobic. In a cross-beta structure, this pattern would result in one side of the domain having a surface rich in hydrophobic side chains which could account for the dimerization of the 120-kD gelation factor subunits.

MeSH Terms
Actinin/analysis,metabolism Actins/metabolism Amino Acid Sequence Animals Base Sequence Binding Sites Carrier Proteins/analysis,metabolism DNA/analysis,genetics Dictyostelium/analysis Dystrophin Microfilament Proteins/analysis,metabolism Molecular Sequence Data Muscle Proteins/analysis,metabolism Protein Conformation
Chemicals
Actins Carrier Proteins Dystrophin Microfilament Proteins Muscle Proteins Actinin abpC protein, Dictyostelium DNA
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Noegel A A
Max-Planck-Institut, Martinsried, Federal Republic of Germany.
Rapp S
Lottspeich F
Schleicher M
Stewart M
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1989-08-00
Pages
607-18
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2115711
Subset
IM
Databases
GENBANK
X15430
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