scholarly journals The amino acid sequence of the D-galactose-binding protein from Escherichia coli B/r.

1981 ◽  
Vol 256 (9) ◽  
pp. 4350-4356 ◽  
Author(s):  
W.C. Mahoney ◽  
R.W. Hogg ◽  
M.A. Hermodson
1983 ◽  
Vol 258 (21) ◽  
pp. 12952-12956 ◽  
Author(s):  
J M Groarke ◽  
W C Mahoney ◽  
J N Hope ◽  
C E Furlong ◽  
F T Robb ◽  
...  

1998 ◽  
Vol 180 (10) ◽  
pp. 2759-2765 ◽  
Author(s):  
Akihito Wada ◽  
Haruo Watanabe

ABSTRACT pbpA, a gene encoding penicillin-binding protein (PBP) 1 of Staphylococcus aureus, was cloned in anEscherichia coli MC1061 transformant which grew on a plate containing 512 μg of vancomycin per ml. This gene encodes a 744-amino-acid sequence which conserves three motifs of PBPs, SXXK, SXN, and KTG. The chromosomal copy of pbpA could be disrupted only when RN4220, a methicillin-sensitive S. aureus strain, had additional copies of pbpA in its episome. Furthermore, these episomal copies of pbpA could not be eliminated by an incompatible plasmid when the chromosomal copy of pbpA was disrupted beforehand. Based on these observations, we concluded that pbpA is essential for the growth of methicillin-sensitive S. aureus.


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