Structure and Function of Nonorthodox Chromatins: II. Preliminary Results on the Localization of Helix-Stabilizing Histone-like Proteins of Thermophilic Archaebacteriae
| Autor: | Bernd Bohrmann, B. Arnold-Schulz-Gahmen, T. Suryanarayana, W. Villiger, D. Searcy, R. Gyalog, Eduard Kellenberger |
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| Rok vydání: | 1990 |
| Předmět: | |
| Zdroj: | Proceedings, annual meeting, Electron Microscopy Society of America. 48:122-123 |
| ISSN: | 2690-1315 0424-8201 |
| DOI: | 10.1017/s0424820100158157 |
| Popis: | Sulfolobus acidocaldarius and Thermoplasma acidophilum prefer extreme living conditions of low pH (60°C) for optimal growth. To resist thermal denaturation of DNA it appears to be associated with helix stabilizing proteins.The chromosomal position of archaebacterial cells (the nucleoid) can be detected as ribosome-free space in which the DNA is located, as is shown by immunocytochemistry (fig. 1a,b). Similar to most eukaryotes the protein- DNA-ratio of their chromatin is relatively high (approx. 1:1 weight by weight), so that no aggregation occurs during dehydration for electron microscopy (fig. 2). Despite this aggregation-insensitivity, (2 and poster 1) the distribution of immunocytochemical label of the DNA bound proteins of Sulfolobus acidocaldarius (hsp's: A,B,C,C') is not exclusively connected with the bulk DNA of the nucleoid; only one of these proteins (C') seems to be associated with the bulk DNA. |
| Databáze: | OpenAIRE |
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