Isolation of the patC gene encoding the cystathionine β-lyase of Lactobacillus delbrueckii subsp bulgaricus and molecular analysis of inter-strain variability in enzyme biosynthesis

被引:20
作者
Aubel, D
Germond, JE
Gilbert, C
Atlan, D
机构
[1] Univ Lyon 1, Unite Microbiol & Genet, UMR 5122, F-69622 Villeurbanne, France
[2] Nestec Ltd, Nestle Res Ctr, CH-1000 Lausanne 26, Switzerland
来源
MICROBIOLOGY-SGM | 2002年 / 148卷
关键词
amino acid catabolism; beta-cystathionase; PatC; lactic acid bacteria; cheesemaking;
D O I
10.1099/00221287-148-7-2029
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The patC gene encoding the cystathionine beta-lyase (CBL) of Lactobacillus delbrueckii subsp. bulgaricus NCDO 1489 was cloned and expressed in Escherichia coli. Overexpression of CBL complemented the methionine auxotrophy of an E. coli metC mutant, demonstrating in vivo that this enzyme functions as a CBL. However, PatC is distinguishable from the MetC CBLs by a low identity in amino acid sequence, a sensitivity to iodoacetic acid, greater thermostability and a lower substrate affinity. Homologues of patC were detected in the 13 Lb. delbrueckii strains studied, but only seven of them showed CBL activity. in constrast to CBL+ strains, all CBL-deficient strains analysed were auxotrophic for methionine. This supports the hypothesis that CBLs from lactobacilli are probably involved in methionine biosynthesis. Moreover, the results of this study suggest that post-transcriptional mechanisms account for the differences in CBL activities observed between strains of Lb. delbrueckii.
引用
收藏
页码:2029 / 2036
页数:8
相关论文
共 37 条
[11]   X-ray structure of MalY from Escherichia coli:: a pyridoxal 5′-phosphate-dependent enzyme acting as a modulator in mal gene expression [J].
Clausen, T ;
Schlegel, A ;
Peist, R ;
Schneider, E ;
Steegborn, C ;
Chang, YS ;
Haase, A ;
Bourenkov, GP ;
Bartunik, HD ;
Boos, W .
EMBO JOURNAL, 2000, 19 (05) :831-842
[12]  
DE MAN J. C., 1960, JOUR APPL BACT, V23, P130, DOI 10.1111/j.1365-2672.1960.tb00188.x
[13]  
Dias B, 1998, APPL ENVIRON MICROB, V64, P3320
[14]   Identification and characterization of a cystathionine β/γ-lyase from Lactococcus lactis ssp cremoris MG1363 [J].
Dobric, N ;
Limsowtin, GKY ;
Hillier, AJ ;
Dudman, NPB ;
Davidson, BE .
FEMS MICROBIOLOGY LETTERS, 2000, 182 (02) :249-254
[15]   CLONING, PURIFICATION, AND CHARACTERIZATION OF BETA-CYSTATHIONASE FROM ESCHERICHIA-COLI [J].
DWIVEDI, CM ;
RAGIN, RC ;
UREN, JR .
BIOCHEMISTRY, 1982, 21 (13) :3064-3069
[16]   A comparative study of volatile compounds in the water-soluble fraction of various types of ripened cheese [J].
Engels, WJM ;
Dekker, R ;
deJong, C ;
Neeter, R ;
Visser, S .
INTERNATIONAL DAIRY JOURNAL, 1997, 7 (04) :255-263
[17]   Partial purification and characterization of two aminotransferases from Lactococcus lactis subsp cremoris B78 involved in the catabolism of methionine and branched-chain amino acids [J].
Engels, WJM ;
Alting, AC ;
Arntz, MMTG ;
Gruppen, H ;
Voragen, AGJ ;
Smit, G ;
Visser, S .
INTERNATIONAL DAIRY JOURNAL, 2000, 10 (07) :443-452
[18]  
Fernández M, 2000, APPL ENVIRON MICROB, V66, P42, DOI [10.1128/AEM.66.1.42-48.2000, 10.1128/AEM.66.10.4200-4204.2000]
[19]  
GENTRYWEEKS CR, 1993, J BIOL CHEM, V268, P7298
[20]   A NEW MOBILE GENETIC ELEMENT IN LACTOBACILLUS-DELBRUECKII SUBSP BULGARICUS [J].
GERMOND, JE ;
LAPIERRE, L ;
DELLEY, M ;
MOLLET, B .
MOLECULAR & GENERAL GENETICS, 1995, 248 (04) :407-416