Molecular characterization of the plasmid‐encoded <i>eps</i> gene cluster essential for exopolysaccharide biosynthesis in <i>Lactococcus lactis</i>

Kranenburg, Richard van; Marugg, Joey D.; Swam, Iris I. van; Willem, Norwin J.; Vos, Willem M. de

doi:10.1046/j.1365-2958.1997.3521720.x

Cited by 232 publications

(230 citation statements)

References 54 publications

Supporting

Mentioning

221

Contrasting

Unclassified

Order By: Relevance

“…Interestingly, proteins CpsC and CpsD share common structural features with the N-terminal and C-terminal regions of Wzc, respectively (14). In fact, this dual sequence similarity is encountered in a variety of pairs of separate proteins in Gram-positive cells, including CpsC/CpsD from S. agalactiae (24), CapA/CapB from S. aureus (26), EpsC/ EpsD from Streptococcus thermophilus (38), and EpsB/EpsA from Lactococcus lactis (39). By contrast, the presence of the N-terminal fragment of protein Wzc from E. coli K12 does not influence the phosphorylation of the C-terminal fragment.…”

Section: Discussionmentioning

confidence: 99%

Tyrosine Phosphorylation of Protein Kinase Wzc fromEscherichia coli K12 Occurs through a Two-step Process

Grangeasse

Doublet

Cozzone

2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

In bacteria, several proteins have been shown to autophosphorylate on tyrosine residues, but little is known on the molecular mechanism of this modification. To get more information on this matter, we have analyzed in detail the phosphorylation of a particular autokinase, protein Wzc, from Escherichia coli K12. The analysis of the hydropathic profile of this protein indicates that it is composed of two main domains: an Nterminal domain, including two transmembrane ␣-helices, and a C-terminal cytoplasmic domain. The C-terminal domain alone can undergo autophosphorylation and thus appears to harbor the protein-tyrosine kinase activity. By contrast, the N-terminal domain is not phosphorylated when incubated either alone or in the presence of the C-domain, and does not influence the extent of phosphorylation of the C-domain. The C-domain contains six different sites of phosphorylation. Among these, five are located at the C-terminal end of the molecule in the form of a tyrosine cluster (Tyr 708 , Tyr 710 , Tyr 711 , Tyr 713 , and Tyr 715 ), and one site is located upstream, at Tyr 569 . The Tyr 569 residue can autophosphorylate through an intramolecular process, whereas the tyrosine cluster cannot. The phosphorylation of Tyr 569 results in an increased protein kinase activity of Wzc, which can, in turn, phosphorylate the five terminal tyrosines through an intermolecular process. It is concluded that protein Wzc autophosphorylates by using a cooperative two-step mechanism that involves both intra-and interphosphorylation. This mechanism may be of biological significance in the signal transduction mediated by Wzc.

show abstract

Section: Discussionmentioning

confidence: 99%

Tyrosine Phosphorylation of Protein Kinase Wzc fromEscherichia coli K12 Occurs through a Two-step Process

Grangeasse

Doublet

Cozzone

2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…To inactivate the mtsA and mntH2 genes in L. plantarum WCFS1 by double cross-over recombination, we used the non-replicating vector pUC18ery (Van Kranenburg et al, 1997). For the introduction of a deletion in mtsA, two fragments flanking the region to be deleted were amplified by PCR.…”

Section: Methodsmentioning

confidence: 99%

Genome-based in silico detection of putative manganese transport systems in Lactobacillus plantarum and their genetic analysis

et al. 2005

View full text Add to dashboard Cite

Manganese serves an important function in Lactobacillus plantarum in protection against oxidative stress and this bacterium can accumulate Mn 2+ up to millimolar levels intracellularly.Although the physiological role of Mn 2+ and the uptake of this metal ion have been well documented, the only uptake system described so far for this bacterium is the Mn 2+ -and Cd 2+-specific P-type ATPase (MntA). Recently, the genome of L. plantarum WCFS1 has been sequenced allowing in silico detection of genes potentially encoding Mn 2+ transport systems, using established microbial Mn 2+ transporters as the query sequence. This genome analysis revealed that L. plantarum WCFS1 encodes, besides the previously described mntA gene, an ABC transport system (mtsCBA) and three genes encoding Nramp transporters (mntH1, mntH2 and mntH3).

show abstract

“…pneumoniae serotype 14 (Kolkman et al, 1997), and WbaP from Sal. enterica (Wang et al, 1996), EpsD from L. lactis NIZO B40 (Van Kranenburg et al, 1997), ExoY from R. meliloti (Mueller et al, 1993) and EpsE from Str. thermophilus Sfi6 (Stingele et al, 1996).…”

Section: Fig 2 Hydrophobicity Plots Of Cpse and Cpse Proteins Frommentioning

confidence: 99%

The complete cps gene cluster from Streptococcus thermophilus NCFB 2393 involved in the biosynthesis of a new exopolysaccharide

et al. 2000

View full text Add to dashboard Cite

The cpsFGHIJKL genes from the cps cluster of Streptococcus thermophilus NCFB 2393 involved in the biosynthesis of EPS were identified, cloned and nucleotide sequenced. The complete cps cluster is contained on an " 11 2 kb chromosomal region which contains 12 ORFs, including the previously cloned cpsABCDE genes. Functions were assigned to some of the predicted gene products on the basis of homology to known sequences as follows : cpsK encodes a protein thought to be involved in the polymerization and export of the polysaccharide ; cpsE, cpsF, cpsG, cpsH, cpsI and cpsJ encode putative sugar transferases. Two insertion sequences, IS1193 and ISS1, were identified within and flanking the 3' end of the cps cluster respectively. Analysis of the expression of the cpsE gene in Escherichia coli demonstrated that it encodes a glucose-1-phosphate transferase ; the enzyme which catalyses the first step in EPS biosynthesis in S. thermophilus NCFB 2393.

show abstract

Molecular characterization of the plasmid‐encoded eps gene cluster essential for exopolysaccharide biosynthesis in Lactococcus lactis

Cited by 232 publications

References 54 publications

Tyrosine Phosphorylation of Protein Kinase Wzc fromEscherichia coli K12 Occurs through a Two-step Process

Tyrosine Phosphorylation of Protein Kinase Wzc fromEscherichia coli K12 Occurs through a Two-step Process

Genome-based in silico detection of putative manganese transport systems in Lactobacillus plantarum and their genetic analysis

The complete cps gene cluster from Streptococcus thermophilus NCFB 2393 involved in the biosynthesis of a new exopolysaccharide

Contact Info

Product

Resources

About