[en] The ponA gene of cosmid L222 of the Mycobacterium leprae genome library encodes a multimodular class A penicillin-binding protein (PBP), PBP1. The PBP, labelled with a polyhistidine sequence, has been produced in Escherichia coli, extracted from the membranes with 3-[(3-cholamidopropyl)-dimethylammonio]-1-propane-sulfonate (CHAPS) and purified by Ni2(+)-nitrilotriacetic acid-agarose chromatography. In contrast to the pon1-encoded class A PBP1, PBP1 undergoes denaturation at temperatures higher than 25 degrees C, it catalyzes acyl transfer reactions on properly structured thiolesters, and it binds penicillin with high affinity.
Research Center/Unit :
CIP - Centre d'Ingénierie des Protéines - ULiège
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Lepage, Sophie; Université de Liège - ULiège > Institut de Chimie > Centre d'Ingénierie des Protéines
Dubois, Philippe ; Université de Liège - ULiège > Institut de Chimie > Centre d'Ingénierie des Protéines
Ghosh, Thushar-Kanti; Université de Liège - ULiège > Institut de Cimie > Centre d'Ingénierie des Protéines
Joris, Bernard ; Université de Liège - ULiège > Centre d'Ingénierie des Protéines
Mahapatra, Sebabrata; Bose Institute-Calcutta > Department of Chemistry
Kundu, Manikuntula; Bose Institute-Calcutta > Department of Chemistry
Basu, Joyoti; Bose Institute-Calcutta > Department of Chemistry
Chakrabarti, Parul; Bose Institute-Calcutta > Department of Chemistry
Cole, Stewart-T; Institut Pasteur (Paris) > Unite de Génétique Moléculaire Bactérienne
Basu, J., S. Mahapatra, M. Kundu, S. Mukhopadhyay, M. Nguyen-Distèche, P. Dubois, B. Joris, J. Van Beeumen, S. T. Cole, P. Chakrabarti, and J.-M. Ghuysen. 1996. Identification and overexpression in Escherichia coli of a Mycobacterium leprae gene, pon1, encoding a high-molecular-mass class A penicillin-binding protein, PBP1. J. Bacteriol. 178:1707-1711.
Broome-Smith, J. K., A. Edelman, S. Yousif, and B. G. Spratt. 1985. The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding proteins 1A and 1B of Escherichia coli K12. Eur. J. Biochem. 147:437-446.
Chambers, H. F., D. Moreau, D. Yajko, C Miick, C. Wagner, C. Hackbarth, S. Kocagöz, E. Rosenberg, W. K. Hadley, and H. Nikaido. 1995. Can penicillins and other β-lactam antibiotics be used to treat tuberculosis? Antimicrob. Agents Chemother. 39:2620-2624.
Eiglmeier, K., N. Honoré, S. A. Woods, B. Caudron, and S. T. Cole. 1993. Use of an ordered cosmid library to deduce the genomic organisation of Mycobacterium leprae. Mol. Microbiol. 7:197-206.
Fraipont, C., M. Adam, M. Nguyen-Distèche, W. Keck, J. Van Beeumen, J. Ayala, B. Granier, H. Hara, and J. M. Ghuysen. 1994. Engineering and overexpression of periplasmic forms of the penicillin-binding protein 3 of Esherichia coli. Biochem. J. 298:189-195.
Frère, J. M., M. Nguyen-Distèche, J. Coyette, and B. Joris. 1992. Mode of action: interaction with the penicillin-binding proteins, p. 148-197. In M. I. Page (ed.), The chemistry of β-lactams. Blackie Academic and Professional, Glasgow, United Kingdom.
Fsihi, H., E. De Rossi, L. Salazar, R. Cantoni, M. Labo, G. Riccardi, H. E. Takiff, K. Eiglmeier, S. Bergh, and S. T. Cole. 1996. Gene arrangement and organization in a ≈76 kb fragment encompassing the oriC region of the chromosome of Mycobacterium leprae. Microbiology 142:3147-3161.
Ghuysen, J. M., P. Charlier, J. Coyette, C. Duez, E. Fonzé, C. Fraipont, C. Goffin, B. Joris, and M. Nguyen-Distèche. 1996. Penicillin and beyond: evolution, protein fold, multimodular polypeptides, and multiprotein complexes. Microb. Drug Resist. 2:163-175.
Grandchamps, J., M. Nguyen-Distèche, C. Damblon, J. M. Frère, and J. M. Ghuysen. 1995. Streptomyces K15 active-site serine DD-transpeptidase: specificity profile for peptide, thiol ester and ester carbonyl donors and pathways of the transfer reactions. Biochem. J. 307:335-339.
Hara, H., and H. Suzuki. 1984. A novel glycan polymerase that synthesizes uncross-linked peptidoglycan in Escherichia coli. FEBS Lett. 168:155-160.
Jamin, M., C. Damblon, S. Millier, R. Hakenbeck, and J. M. Frère. 1993. Penicillin-binding protein 2x of Streptococcus pneumoniae: enzymic activities and interactions with β-lactams. Biochem. J. 292:735-741.
Nguyen-Distèche, M., M. Leyh-Bouille, S. Pirlot, J. M. Frère, and J. M. Ghuysen. 1986. Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carhonyl donors. Biochem. J. 235:167-176.
Palomeque-Messia, P., S. Englebert, M. Leyh-Bouille, M. Nguyen-Distèche, C. Duez, S. Houba, O. Dideberg, J. Van Beeumen, and J. M. Ghuysen. 1991. Amino acid sequence of the penicillin-binding protein/DD-peptidase of Streptomyces K15. Biochem. J. 279:223-230.
Rees, R. J. W. 1985. The microbiology of leprosy, p. 31-52. In R. C. Hastings (ed.), Churchill Livingstone, Edinburgh, United Kingdom.
Spratt, B. G., J. Zhou, M. Taylor, and M. J. Merrick. 1996. Monofunctional biosynthetic peptidoglycan transglycosylases. Mol. Microbiol. 19:639-647.