CHARACTERIZATION OF THE PASTEURELLA-MULTOCIDA SKP AND FIRA GENES

被引：11

作者：

DELAMARCHE, C

MANOHA, F

BEHAR, G

HOULGATTE, R

HELLMAN, U

WROBLEWSKI, H

机构：

[1] UNIV RENNES 1,DEPT MEMBRANES & OSMOREGULAT,CNRS,URA 256,F-35042 RENNES,FRANCE

[2] CNRS,UPR 420,VILLEJUIF,FRANCE

[3] LUDWIG INST CANC RES,S-75124 UPPSALA,SWEDEN

来源：

GENE | 1995年 / 161卷 / 01期

关键词：

DNA SEQUENCING; N-TERMINAL AMINO-ACID SEQUENCE; AMINO-ACID HOMOLOGY; LIPID SYNTHESIS; PORIN;

D O I：

10.1016/0378-1119(95)00254-4

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

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 fir A gene of Ec. The skp and fir A 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.

引用

页码：39 / 43

页数：5

共 19 条

[1]

Chanter N, 1989, PASTEURELLA PASTEURE, P161

[2] PURIFICATION AND CHARACTERIZATION OF PROTEIN-H, THE MAJOR PORIN OF PASTEURELLA-MULTOCIDA [J].