THE ENTEROCOCCUS-HIRAE R40 PENICILLIN-BINDING PROTEIN-5 AND THE METHICILLIN-RESISTANT STAPHYLOCOCCUS-AUREUS PENICILLIN-BINDING PROTEIN 2' ARE SIMILAR

被引:48
作者
ELKHARROUBI, A
JACQUES, P
PIRAS, G
VANBEEUMEN, J
COYETTE, J [1 ]
GHUYSEN, JM
机构
[1] STATE UNIV LIEGE,INST CHIM,CTR INGENIERIE PROT,B6,B-4000 LIEGE,BELGIUM
[2] STATE UNIV GHENT,MICROBIOL & MICROBIELE GENET LAB,B-9000 GHENT,BELGIUM
关键词
D O I
10.1042/bj2800463
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The penicillin-resistant Enterococcus hirae R40 has a typical profile of membrane-bound penicillin-binding proteins (PBPs) except that the 71 kDa PBP5 of low penicillin affinity represents about 50% of all the PBPs present. Water-soluble tryptic-digest peptides were selectively produced from PBP5, their N-terminal regions were sequenced and synthetic oligonucleotides were used as primers to generate a 476 bp DNA fragment by polymerase chain reaction. On the basis of these data, the PBP5-encoding gene was cloned in Escherichia coli by using pBR322 as vector. The gene, included in a 7.1 kb insert, had the information for a 678-amino acid-residue protein. PBP5 shows similarity, in the primary structure, with the high-molecular-mass PBPs of class B. In particular, amino acid alignment of the enterococcal PBP5 and the methicillin-resistant staphylococcal PBP2' generates scores that are 30, for the N-terminal domains, and 53, for the C-terminal domains, standard deviations above that expected for a run of 20 randomized pairs of proteins having the same amino acid compositions as the two proteins under consideration.
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页码:463 / 469
页数:7
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