Gottler, Thomas and Holler, Eggehard (2006) Screening for beta-poly(L-malate) binding proteins by affinity chromatography. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 341 (4). pp. 1119-1127. ISSN 0006-291X, 1090-2104
Full text not available from this repository. (Request a copy)Abstract
Pely(beta-L-malic acid) is a cell type-specific polymer of myxomycetes (true slime molds) with the physiological role to organize mobility of certain proteins over the giant multinucleated plasmodia. We have developed an affinity chromatography employing 1,6-diamino-n-hexane-Sepharose-coupled poly(malic acid) to identify such proteins in cellular extracts of Physarum polycephalum. Molecular masses were measured by SDS-PAGE and non-denaturing PAGE after silver staining and/or Western blotting. Protein complexes/subunits were detected by 2-dimensional non-denaturing PAGE/SDS-PAGE. A simplified gel shift experiment displayed binding to fragmented calf thymus DNA. Nuclei were richest in poly(malate) binding proteins followed by cytoplasm and membranes. A protein of 370 kDa dissociated into 11 subunits of 11-29 kDa, indicative of a highly complex protein. This and other proteins displayed binding to nucleic acid in gel shift experiments. Poly(malate) is considered a structural and functional equivalent of long contiguous aspartate repeats in proteins of eukaryotes. (c) 2006 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | DNA-POLYMERASE-ALPHA; POLY-L-MALATE; PHYSARUM-POLYCEPHALUM; CELL-CYCLE; POLYACRYLAMIDE GELS; SUBUNIT STRUCTURE; RICH PROTEIN; PLASMODIUM; ACID; SEQUENCE; Physarum polycephalum; poly(malic acid); poly(malic acid) binding proteins; affinity chromatography; poly(malate)-aminohexyl-sepharose; myxomycete; plasmodium; nuclear synchrony; molecular mimicry; poly(aspartic acid) |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Alumni or Retired > Prof. Dr. Eggehard Holler |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 17 Feb 2021 12:23 |
| Last Modified: | 17 Feb 2021 12:23 |
| URI: | https://pred.uni-regensburg.de/id/eprint/34777 |
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