Delamarche C, Manoha F, Béhar G, Houlgatte R, Hellman U, Wróblewski H
Département Membranes et Osmorégulation, Centre National de la Recherche Scientifique, Rennes, France.
Gene. 1995 Aug 8;161(1):39-43. doi: 10.1016/0378-1119(95)00254-4.
A 2.9-kb fragment of the Pasteurella multocida (Pm) genome encoding proteins p25 (25 kDa) and p28 (28 kDa) has previously been cloned and expressed in Escherichia coli (Ec). In the present paper, the nucleotide (nt) sequence of a 1.8-kb subfragment encoding the two proteins is described. The cloned fragment contains three open reading frames (ORFs). ORF1 is incomplete. ORF2 is homologous to the skp gene of Ec. ORF3 overlaps ORF2 and is highly homologous to the firA gene of Ec. The skp and firA genes are part of an operon governing the first steps of lipid A synthesis. Comparing the nt sequence with the N-terminal sequences of p25 and p28 revealed that the two proteins are encoded by ORF2 (skp). The preprotein p28 is converted into p25 by cleavage of a 23-amino-acid leader peptide. Though it serologically cross-reacts with porin H of Pm, p25 is not related to known bacterial porins.
多杀性巴氏杆菌(Pm)基因组中一个编码p25(25 kDa)和p28(28 kDa)蛋白的2.9 kb片段先前已被克隆并在大肠杆菌(Ec)中表达。在本文中,描述了一个编码这两种蛋白的1.8 kb亚片段的核苷酸(nt)序列。克隆片段包含三个开放阅读框(ORF)。ORF1不完整。ORF2与Ec的skp基因同源。ORF3与ORF2重叠,且与Ec的firA基因高度同源。skp和firA基因是控制脂质A合成第一步的操纵子的一部分。将nt序列与p25和p28的N端序列进行比较,发现这两种蛋白由ORF2(skp)编码。前体蛋白p28通过切割一个23个氨基酸的前导肽转化为p25。尽管p25与Pm的孔蛋白H有血清学交叉反应,但它与已知的细菌孔蛋白无关。