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001-es BibID:	BIBFORM046867
Első szerző:	Itoh, Masayoshi
Cím:	Proteins that interact with GTP in Streptomyces griseus and its possible implication in morphogenesis / Itoh Masayoshi, Penyige Andras, Okamoto Susumu, Ochi Kozo
Dátum:	1996
ISSN:	0378-1097
Megjegyzések:	By cross-linking with [?-32P]GTP or [?-32P]GTP with or without UV treatment, several proteins of Streptomyces griseus were shown to interact with GTP in specific ways. After gel electrophoresis, 19 bands of radioactivity were found; 12 bands were assigned as GTP-binding proteins and 6 bands as phosphorylated proteins. One band was assumed to be a guanylylated protein. The profile of radioactive bands was similar between cells prepared from liquid or solid culture, but markedly different between growth phases. A mutant (strain M-1) defective in aerial mycelium formation, which was originally found as a decoyinine-resistant isolate, was found to have a different profile of phosphorylated proteins.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Fems Microbiology Letters. - 135 : 2-3 (1996), p. 311-316. -
További szerzők:	Penyige András (1954-) (molekuláris genetikus) Okamoto, Susumu Ochi, Kozo
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM046865
Első szerző:	Ochi, Kozo
Cím:	The possible role of ADP-ribosylation in sporulation and streptomycin production by Streptomyces griseus / Ochi, K., Penyige, A., Barabás, Gy.
Dátum:	1992
ISSN:	0022-1287
Megjegyzések:	Mutants resistant to 3-aminobenzamide, a known inhibitor of ADP-ribosyltransferase, were obtained from Streptomyces griseus IFO 13189, a streptomycin-producing strain. One (strain no. 4), which had significantly reduced ADP-ribosyltransferase activity, was analysed in detail. Mutant 4 displayed a conditional phenotype with respect to cultivation temperature. At 30 degrees C, it exhibited severely reduced ability to produce aerial mycelium (on solid medium) and submerged spores and streptomycin (in liquid culture), but this ability was fully restored at 25 degrees C. The mutant produced A-factor normally, regardless of cultivation temperature, and exhibited normal ability to accumulate ppGpp intracellularly. SDS-PAGE analyses of cellular proteins labelled by [32P]NAD revealed that an ADP-ribosylated protein with a molecular size of 44 kDa, which appeared in sporulating cultures of the parent strain, was missing from the mutant grown at the non-permissive temperature (30 degrees C). Genetic analysis showed that the aba mutation conferring resistance to 3-aminobenzamide was tightly linked to the altered phenotype. Failure to ADP-ribosylate certain cellular protein(s), presumably due to the aba mutation, may be responsible for impaired differentiation in this mutant.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of General Microbiology. - 138 : (Pt8) (1992), p. 1745-1750. -
További szerzők:	Penyige András (1954-) (molekuláris genetikus) Barabás György (1933-) (sejtbiológus, molekuláris genetikus)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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