Structure of peptidoglycan from Thermus thermophilus HB8

Quintela, José Carlos; Pittenauer, Ernst; Allmaier, Günter; Arán, Vicente J.; Pedro, Miguel A. de

doi:10.1128/jb.177.17.4947-4962.1995

Cited by 74 publications

(100 citation statements)

References 59 publications

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“…Ornithine is an intermediate of arginine biosynthesis. Furthermore, the compound is also used as a precursor of polyamines that were involved in cellular processes and an indispensable component of the cell wall in T. thermophilus [24,25]. Requirement of ornithine for several cellular functions may have developed several supporting systems to produce ornithine.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27

et al. 2002

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We conducted a chromosome walk to obtain a DNA fragment downstream of lysJ and found an argE homolog in a putative operon composed of lysJ^orfC^orfD^argE homologs. A knockout mutant of the argE homolog showed significantly slow growth on a minimal medium, and the growth was markedly improved by addition of lysine. We therefore termed this gene lysK. Purified LysK protein has deacetylating activities for both N 2 -acetyllysine and N 2 -acetylornithine at almost equal efficiency. These results suggest that lysK which may share an ancestor with argE functions not only for the lysine biosynthesis, but also for arginine biosynthesis in Thermus thermophilus. ß 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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Section: Discussionmentioning

confidence: 99%

Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27

et al. 2002

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“…Positive-and negative-ion plasma desorption spectra were obtained using plasma desorption linear time-of-flight mass spectrometry (PDMS) as described (Allmaier et al, 1992;Allmaier and Schmid, 1993;Quintela et al, 1995b).…”

Section: Mass Spectrometry Of Muropeptidesmentioning

confidence: 99%

Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells

Zöllner

et al. 1997

Molecular Microbiology

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SummaryThe cell wall structure of Salmonella typhimurium has been studied for the first time during transit from freeliving to parasitic lifestyles. Peptidoglycan of S. typhimurium proliferating within human epithelial cells contains a high proportion of previously unidentified muropeptides (5-10-fold higher than in extracellular bacteria). Amino acid and mass-spectrometry analyses showed that these new components consist of

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“…The filter was incubated for 16 h at 4ЊC in a renaturation buffer containing 20 mM Tris-ClH, 150 mM NaCl, 2.5 mM dithiothreitol, 2.5% (vol/vol) Nonidet P-40, 10% (vol/vol) glycerol, and 5% skim milk (pH 7.5) with three buffer changes and washed in binding buffer (10 mM Tris-ClH, 50 mM NaCl, 1 mM EDTA, 1 mM dithiothreitol, 5% [vol/vol] glycerol, and 0.125% [wt/vol] skim milk [pH 8]). The membrane was incubated at 25ЊC for 3 h in binding buffer containing a sonicated peptidoglycan fraction (24 g/ml in Ornitin equivalents) from T. thermophilus HB8 (24) and was washed again in the same buffer. Peptidoglycan bound to proteins was detected as described above with a specific anti-peptidoglycan rabbit antiserum generously given by H. Schwarz.…”

Section: Methodsmentioning

confidence: 99%

A conserved motif in S-layer proteins is involved in peptidoglycan binding in Thermus thermophilus

et al. 1996

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There is experimental evidence to suggest that the 100-kDa S-layer protein from Thermus thermophilus HB8 binds to the peptidoglycan cell wall. This property could be related to the presence of a region ( Paracrystalline surface layers (S-layers) are commonly found within prokaryotes belonging to different phylogenetic groups (22). As the outermost envelope, the functions of S-layers are related to their interaction with the specific environment in which these organisms grow. However, their constant presence in bacteria belonging to the oldest phylogenetic groups and the severe defects shown by S-layer-defective mutants in these groups (13, 17) suggest that primitive S-layers could have played a role essentially related to the maintenance of the cell morphology and envelope integrity (2, 22).Three-dimensional reconstruction of S-layers has revealed features common among them (22), independently of differences in their specific functions. Essentially, S-layers present a smooth surface which faces outside and a more corrugated one that binds them to the underlying envelope, whatever its nature (peptidoglycan, outer membrane, or lipopolysaccharide). At higher resolution, this corrugated side shows up as wide columns, located at the main symmetry axis, that are interconnected through a network of thin contacts at the surface. This network of contacts generates the smooth face of the S-layer.This common morphology of the S-layer is built up by a single protein component that is folded in at least two clear domains: a heavy domain, which interacts with other equivalent domains to form the wide columns that bind the S-layer to the cell, and one or more light domains to connect them at the surface (28). However, the resolution of the three-dimensional models available at present does not allow a correlation between structural topology and protein sequence to be made. In addition, the scarcity of both S-layer models and protein sequences and the high divergence found within the latter do not in general allow association of specific sequence motifs or patterns with specific structural features. However, in a recent article, Lupas et al. (20) have described the existence of one or more copies of a protein domain known as the S-layer homology (SLH) region in a number of S-layers and regular membrane proteins from unrelated bacteria. On the basis of the homology, also found with extracellular enzymes from grampositive bacteria (20), a peptidoglycan-binding function was tentatively assigned to this domain.Despite belonging to a phylogenetic group different from that of gram positive bacteria, the 100-kDa S-layer protein from Thermus thermophilus HB8 was included among those that contain an SLH domain (11,20). In this 917-amino-acidlong protein (SlpA), the SLH domain was found from amino acid positions 28 to 87, thus suggesting the possibility of an interaction in vivo between the S-layer and the peptidoglycan. Two biochemical data can be argued to support the existence of such interactions. First, the solubilization of SlpA w...

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Structure of peptidoglycan from Thermus thermophilus HB8

Abstract: The composition and structure of peptidoglycan (murein) extracted from the extreme thermophilic eubacterium Thermus thermophilus HB8 are presented. The structure of 29 muropeptides, accounting for more than 85% of total murein, is reported.

Cited by 74 publications

References 59 publications

Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27

Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27

Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells

A conserved motif in S-layer proteins is involved in peptidoglycan binding in Thermus thermophilus

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