Specificity and selectivity determinants of peptide transport in Lactococcus lactis and other microorganisms

被引:77
作者
Doeven, MK
Kok, J
Poolman, B
机构
[1] Univ Groningen, Dept Biochem, Groningen Biomol Sci & Biotechnol Inst, NL-9747 AG Groningen, Netherlands
[2] Univ Groningen, Dept Genet, Groningen Biomol Sci & Biotechnol Inst, NL-9751 NN Haren, Netherlands
关键词
D O I
10.1111/j.1365-2958.2005.04698.x
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
Peptide transport in microorganisms is important for nutrition of the cell and various signalling processes including regulation of gene expression, sporulation, chemotaxis, competence and virulence development. Peptide transport is mediated via different combinations of ion-linked and ATP-binding cassette (ABC) transporters, the latter utilizing single or multiple peptide-binding proteins with overlapping specificities. The paradigm for research on peptide transport is Lactococcus lactis, in which the uptake of peptides containing essential amino acids is vital for growth on milk proteins. Differential expression and characteristics of peptide-binding proteins in several Lactococcus lactis strains resulted in apparent conflicts with older literature. Recent developments and new data now make the pieces of the puzzle fall back into place again and confirm the view that the oligopeptide-binding proteins determine the uptake selectivity of their cognate ABC transporters. Besides reviewing the current data on binding specificity and transport selectivity of peptide transporters in L. lactis, the possible implications for peptide utilization by other bacterial species are discussed.
引用
收藏
页码:640 / 649
页数:10
相关论文
共 47 条
[41]   Genetic and functional characterization of dpp genes encoding a dipeptide transport system in Lactococcus lactis [J].
Sanz, Y ;
Lanfermeijer, FC ;
Renault, P ;
Bolotin, A ;
Konings, WN ;
Poolman, B .
ARCHIVES OF MICROBIOLOGY, 2001, 175 (05) :334-343
[42]  
SANZ Y, 2005, IN PRESS INT J FOOD
[43]   Activation of the Bacillus subtilis global regulator CodY by direct interaction with branched-chain amino acids [J].
Shivers, RP ;
Sonenshein, AL .
MOLECULAR MICROBIOLOGY, 2004, 53 (02) :599-611
[44]  
TAME JRH, 1994, SCIENCE, V264, P1578, DOI 10.1126/science.8202710
[45]   Identification of a differentially expressed oligopeptide binding protein (OppA2) in Streptococcus uberis by representational difference analysis of cDNA [J].
Taylor, DL ;
Ward, PN ;
Rapier, CD ;
Leigh, JA ;
Bowler, LD .
JOURNAL OF BACTERIOLOGY, 2003, 185 (17) :5210-5219
[46]   GENETIC AND BIOCHEMICAL-CHARACTERIZATION OF THE OLIGOPEPTIDE TRANSPORT-SYSTEM OF LACTOCOCCUS-LACTIS [J].
TYNKKYNEN, S ;
BUIST, G ;
KUNJI, E ;
KOK, J ;
POOLMAN, B ;
VENEMA, G ;
HAANDRIKMAN, A .
JOURNAL OF BACTERIOLOGY, 1993, 175 (23) :7523-7532
[47]   Analysis of differences in the functional properties of the substrate binding proteins of the Borrelia burgdorferi oligopeptide permease (opp) operon [J].
Wang, XG ;
Kidder, JM ;
Scagliotti, JP ;
Klempner, MS ;
Noring, R ;
Hu, LDT .
JOURNAL OF BACTERIOLOGY, 2004, 186 (01) :51-60