OCCURRENCE OF DIPHTHAMIDE IN ARCHAEBACTERIA
OCCURRENCE OF DIPHTHAMIDE IN ARCHAEBACTERIA
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DOI:
10.1128/jb.153.3.1342-1347.1983
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发表时间:
1983-01-01
影响因子:
3.2
通讯作者:
BODLEY, JW
中科院分区:
文献类型:
--
作者:
PAPPENHEIMER, AM;DUNLOP, PC;BODLEY, JW
The nature of the diphtheria toxin fragment A recognition site in the protein synthesis translocating factor present in cell-free preparations from the archaebacteria Thermoplasma acidophilum and Halobacterium halobium was examined. In agreement with earlier work it was found that extracts from these organisms contain a protein factor which is a substrate for the ADP-ribosylation reaction catalyzed by diphtheria toxin fragment A. The rate of the reaction was .apprx. 1000 times slower than that typically observed with eukaryotic elongation factor 2. The presence of diphthine (the deamidated form of diphthamide, i.e., 2-[3-carboxyamide-3-(trimethylammonio)propyl]histidine) was demonstrated in acid hydrolysates of H. halobium protein in amounts comparable to those found in hydrolysates of similar preparations from eukaryotic cells (Saccharomyces cerevisiae and HeLa [human cervical carcinoma]). Diphthine could not be detected in hydrolysates of protein from the eubacterium Escherichia coli. Whereas archaebacterial eukaryotic elongation factors contain diphthamide, they differ importantly in other respects.