Wodara C, Kostka S, Egert M, Kelly D P, Friedrich C G
Lehrstuhl für Technische Mikrobiologie, Fachbereich Chemietechnik, Universität Dortmund, Germany.
J Bacteriol. 1994 Oct;176(20):6188-91. doi: 10.1128/jb.176.20.6188-6191.1994.
The coding region for lithotrophic sulfur oxidation (Sox) in Paracoccus denitrificans GB17 was identified by isolation of a transposon Tn5-mob mutant with a Sox- phenotype (strain TP19). The corresponding wild-type region was cloned previously (G. Mittenhuber, K. Sonomoto, M. Egert, and C. G. Friedrich, J. Bacteriol. 173:7340-7344, 1991). Sequence analysis of a 2.5-kb subclone that complemented strain TP19 revealed that Tn5-mob was inserted into a coding region for a 553-amino-acid polypeptide named SoxB. This polypeptide had an M(r) of 60.573, including a possible signal peptide. The function of the SoxB protein of P. denitrificans GB17 appeared to be identical to that of enzyme B of the thiosulfate-oxidizing enzyme system of Thiobacillus versutus. The amino acid compositions of the two proteins were identical, and the amino acid sequences of three internal peptides of enzyme B as determined by Edman degradation were identical to corresponding sequences of the deduced SoxB protein of P. denitrificans GB17.
通过分离具有硫氧化缺陷型(Sox-)表型的转座子Tn5-mob突变体(菌株TP19),确定了反硝化副球菌GB17中嗜石性硫氧化(Sox)的编码区域。相应的野生型区域先前已被克隆(G. Mittenhuber、K. Sonomoto、M. Egert和C. G. Friedrich,《细菌学杂志》173:7340-7344,1991年)。对互补菌株TP19的一个2.5 kb亚克隆进行序列分析,结果显示Tn5-mob插入到了一个编码名为SoxB的553个氨基酸多肽的区域。该多肽的分子量为60.573,包括一个可能的信号肽。反硝化副球菌GB17的SoxB蛋白的功能似乎与维氏硫杆菌硫代硫酸盐氧化酶系统的酶B相同。这两种蛋白质的氨基酸组成相同,通过埃德曼降解法测定的酶B的三个内部肽段的氨基酸序列与反硝化副球菌GB17推导的SoxB蛋白的相应序列相同。