Structure and function of proteins of the phosphotransferase system and of 6-phospho-Î²-glycosidases in Gram-positive bacteria

James Baddiley was a biochemist who used the methods and insight of the organic chemist to answer important questions in biology, notably coenzyme structure and the structure and function of bacterial cell walls. A graduate of Manchester University, he moved to Cambridge in 1944 with A. R. Todd, where he synthesized adenosine triphosphate, the nucleotide concerned with essential energy transformations in all forms of life. As an independent researcher at the Lister Institute in London he elucidated the structure of coenzyme A and other coenzymes. He was appointed Professor of Organic Chemistry in Newcastle, where the exploration of the structures of two cytidine nucleotides led to the discovery of the teichoic acids, major components of the cell walls and membranes of Gram-positive bacteria. These discoveries were extended to cover the structures, biosynthesis, function and immunology of the teichoic acids. Baddiley became Professor of Chemical Microbiology in 1977. Moving to Cambridge after his retirement, he was able to continue his researches in the Department of Biochemistry. He was elected a Fellow of Pembroke College and as an elder statesman undertook extensive committee work, often as chairman, both in Cambridge University and nationally. He was knighted in 1977.

Download Full-text

Lipoteichoic Acid Synthesis and Function in Gram-Positive Bacteria

Annual Review of Microbiology ◽

10.1146/annurev-micro-091213-112949 ◽

2014 ◽

Vol 68 (1) ◽

pp. 81-100 ◽

Cited By ~ 178

Author(s):

Matthew G. Percy ◽

Angelika Gründling

Keyword(s):

Lipoteichoic Acid ◽

Acid Synthesis ◽

Gram Positive ◽

Gram Positive Bacteria ◽

And Function

Download Full-text

CcpA-Dependent Carbon Catabolite Repression in Bacteria

Microbiology and Molecular Biology Reviews ◽

10.1128/mmbr.67.4.475-490.2003 ◽

2003 ◽

Vol 67 (4) ◽

pp. 475-490 ◽

Cited By ~ 176

Author(s):

Jessica B. Warner ◽

Juke S. Lolkema

Keyword(s):

Catabolite Repression ◽

Carbon Catabolite Repression ◽

Serine Phosphorylation ◽

Regulation System ◽

Sequence Motif ◽

Phosphotransferase System ◽

Gram Positive ◽

The Public ◽

Gram Positive Bacteria ◽

Close Phylogenetic Relationship

SUMMARY Carbon catabolite repression (CCR) by transcriptional regulators follows different mechanisms in gram-positive and gram-negative bacteria. In gram-positive bacteria, CcpA-dependent CCR is mediated by phosphorylation of the phosphoenolpyruvate:sugar phosphotransferase system intermediate HPr at a serine residue at the expense of ATP. The reaction is catalyzed by HPr kinase, which is activated by glycolytic intermediates. In this review, the distribution of CcpA-dependent CCR among bacteria is investigated by searching the public databases for homologues of HPr kinase and HPr-like proteins throughout the bacterial kingdom and by analyzing their properties. Homologues of HPr kinase are commonly observed in the phylum Firmicutes but are also found in the phyla Proteobacteria, Fusobacteria, Spirochaetes, and Chlorobi, suggesting that CcpA-dependent CCR is not restricted to gram-positive bacteria. In the α and β subdivisions of the Proteobacteria, the presence of HPr kinase appears to be common, while in the γ subdivision it is more of an exception. The genes coding for the HPr kinase homologues of the Proteobacteria are in a gene cluster together with an HPr-like protein, termed XPr, suggesting a functional relationship. Moreover, the XPr proteins contain the serine phosphorylation sequence motif. Remarkably, the analysis suggests a possible relation between CcpA-dependent gene regulation and the nitrogen regulation system (Ntr) found in the γ subdivision of the Proteobacteria. The relation is suggested by the clustering of CCR and Ntr components on the genome of members of the Proteobacteria and by the close phylogenetic relationship between XPr and NPr, the HPr-like protein in the Ntr system. In bacteria in the phylum Proteobacteria that contain HPr kinase and XPr, the latter may be at the center of a complex regulatory network involving both CCR and the Ntr system.

Download Full-text

The role of phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, in the regulation of carbon metabolism in gram-positive bacteria

Journal of Cellular Biochemistry ◽

10.1002/jcb.240510105 ◽

1993 ◽

Vol 51 (1) ◽

pp. 19-24 ◽

Cited By ~ 37

Author(s):

Jonathan Reizer ◽

Antonio H. Romano ◽

Josef Deutscher

Keyword(s):

Carbon Metabolism ◽

Phosphotransferase System ◽

Gram Positive ◽

Gram Positive Bacteria

Download Full-text

The structure and function of HPr

Biochemistry and Cell Biology ◽

10.1139/o98-043 ◽

1998 ◽

Vol 76 (2-3) ◽

pp. 359-367 ◽

Cited By ~ 12

Author(s):

E Bruce Waygood

Keyword(s):

Structure And Function ◽

Side Chain ◽

Phosphoryl Group ◽

Phosphotransferase System ◽

Tertiary Structures ◽

E Coli ◽

H Nmr ◽

Early Protein ◽

Alpha Beta ◽

And Function

Histidine-containing phosphocarrier protein, HPr, was one of the early protein tertiary structures determined by two-dimensional 1H-NMR. Tertiary structures for HPrs from Escherichia coli, Bacillus subtilis, and Staphylococcus aureus have been obtained by 1H NMR and the overall folding pattern of HPr is highly conserved, a beta alpha beta beta alpha beta alpha arrangement of three alpha-helices overlaying a four-stranded beta-sheet. High-resolution structures for HPrs from E. coli and B. subtilis have been obtained using 15N- and 13C-labeled proteins. The first application of NMR to the understanding of the structure and function of HPr was to describe the phosphohistidine isomer, Ndelta1-P-histidine in S. aureus phospho-HPr, and the unusual pKas of the His-15 side chain. The pKa values for the His-15 imidazole from more recent studies are 5.4 for HPr and 7.8 for phospho-HPr from E. coli, for example. A consensus description of the active site is proposed for HPr and phospho-HPr. In HPr, His-15 has a defined conformation and N-caps helix A, and is thus affected by the helix dipole. His-15 undergoes a small conformational change upon phosphorylation, a movement to allow the phosphoryl group to be positioned such that it forms hydrogen bonds with the main chain amide nitrogens of residue 16 (not conserved) and Arg-17. Interactions between residue 12 side chain (not conserved: asparagine, serine, and threonine) and His-15, and between the Arg-17 guanidinium group and the phosphoryl group, are either weak or transitory.Key words: HPr, NMR, phosphoenolpyruvate:sugar phosphotransferase system, phosphohistidine, phosphoserine.

Download Full-text