Angerer, Bernhard and Holler, Eggehard (1995) Large complexes of .beta.-poly(L-malate) with DNA polymerase .alpha., histones, and other proteins in nuclei of growing plasmodia of Physarum polycephalum. BIOCHEMISTRY, 34 (45). pp. 14741-14751. ISSN 0006-2960
Full text not available from this repository.Abstract
Of the various cell types in the life cycle of Physarum polycephalum, only the growing plasmodium contains the unusual polyester beta-poly(L-malate). The nuclei exhibit large complexes of this polymer with nuclear proteins, among them DNA polymerase alpha, histones, and HMG-like proteins. The complexes are indicated by the results of size exclusion chromatography and chemical cross-linking with 1-ethyl-3-[3-(dimethylamino)propyl]carbo hydrochloride (EDC). After hydroxylaminolysis of the cross-linked polyester, the proteins are liberated and visualized on Western blots. The complexes of 1200-1400 kDa molecular mass exceed by far the size of free beta-poly(L-malate) and proteins. The observed variation in mass appears to be mainly a function of the kind and stoichiometry of the protein constituents and may explain the relatively high molecular mass in S phase and the low molecular mass during G2 phase of the mitotic cycle. The complexes are considerably stable at moderate ionic strength (100 mM KCl). Also, endogenous beta-poly(L-malate) does not exchange with added beta-[C-14]poly(L-malate) during the lysis of the nuclei and the sample preparation. The complexes are dissociated at elevated concentrations of KCl, in the presence of spermine hydrochloride, or by treatment with DEAE/cellulose. Available evidence indicates that beta-poly(L-malate) may be involved in the maintenance of the plasmodial state of P. polycephalum.
Item Type: | Article |
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Uncontrolled Keywords: | CELL-CYCLE; NUCLEOPLASMIN; CLEAVAGE; SEQUENCE; PRIMASE; ACID; GELS |
Subjects: | 500 Science > 540 Chemistry & allied sciences 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 Nov 2023 10:53 |
Last Modified: | 17 Nov 2023 10:53 |
URI: | https://pred.uni-regensburg.de/id/eprint/52208 |
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