| | 1 | Author
| K. L. Friedm, R. Egel | Requires cookie* | | | Title
| Protein Patterns during Sporulation in Fission Yeast  | | | | Abstract
| Various strains (wild-type and m utants) of Schizosaccharom yces pom be were subjected to sporulation conditions, and analysed with regard to changes in their protein patterns. Trisbuffer-soluble proteins (TS) and DNA-binding proteins (DB) were denatured and separated by poly acrylam ide electrophoresis. A fter endogenous nitrogen depletion (the apparent trigger of conjuga tion and sporulation) the following alterations were observed: larger TS-proteins were proteolytical-ly degraded; the pattern of DB-proteins underwent several selective changes (reduction, enforce ment, or new appearance of individual bands) ; an endonucleolytic DNase activity appeared. Most of these changes were expressed before conjugation, and did not appear in sterile strains. They could, however, be provoked by an abrupt shift to nitrogen-free medium, even in sterile strains. Inhibition studies with cycloheximide revealed at least two phases of protein synthesis specifically needed for sporulation: a very sensitive phase before conjugation, and a more resistant phase lasting until 0.5 h before spore form ation. Medium exchange between heterothallic cultures (h+ and h~) effected certain sporulation-specific alterations of the DB-protein pattern, indicative of diffusible mating-type factors in the culture fluid. | | | |
Reference
| Z. Naturforsch. 33c, 84 (1978); received December 14 1977 | | | |
Published
| 1978 | | | |
Keywords
| Schizosaccharom yces pom be, Conjugation, Sporulation, Endonuclease, Gel Electrophoresis | | | |
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| default:Reihe_C/33/ZNC-1978-33c-0084.pdf | | | | Identifier
| ZNC-1978-33c-0084 | | | | Volume
| 33 | |
| 2 | Author
| Zsuzsa Izsvák, Zsolt Jobbágy, Ernö Duda | Requires cookie* | | | Title
| Purification and Characterization of Ceql Restriction Endonuclease | | | | Abstract
| C eql, a type II restriction endonuclease, an isoschizomer of EcoRV was purified to apparent homogeneity by a combination of salt precipitation, ion exchange, dye affinity and hydrophobic interaction chromatographies. The crude enzyme was present in the form of large aggregates that could be pelleted by high speed centrifugation. The enzyme was not associated with cellular membranes, though non-ionic detergents lowered the apparent size of the aggregates. The puri fied enzyme also showed a tendency to form large molecular mass (66-600 kDa) complexes under physiological conditions, in the absence of cleavable DN A. The enzyme formed smaller complexes in the presence of D N A and non-ionic detergents and dissociated into subunits (and undergoes reversible loss of activity) in the presence of high concentrations of salts. According to SDS gel electrophoresis and sedimentation analysis the molecular mass of the monomer 32 ± 2 kDa. The enzyme had a rather broad pH optimum, extending into the alka line range and lost specificity and activity in buffers below pH 6. | | | |
Reference
| Z. Naturforsch. 47c, 830—834 (1992); received May 26/ | | | |
Published
| 1992 | | | |
Keywords
| Restriction Enzyme, Endonuclease, Purification, Corynebacterium, Multimeric Enzyme | | | |
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| default:Reihe_C/47/ZNC-1992-47c-0830.pdf | | | | Identifier
| ZNC-1992-47c-0830 | | | | Volume
| 47 | |
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