Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment.

Li, Shun‐Cheng; Goto, Natalie K.; Williams, Karen A.; Deber, Charles M.

doi:10.1073/pnas.93.13.6676

Cited by 285 publications

(235 citation statements)

References 54 publications

Supporting

Mentioning

225

Contrasting

Unclassified

Order By: Relevance

“…This implies that the amino-acid substitutions in TagE of EvoR1, EvoR3 and EvoI2 are detrimental for its function. This could be expected from the L436P substitution in EvoI2, where the proline may act as a secondary-structure breaker (Li et al, 1996). Apparently, a K360R aminoacid substitution is also detrimental, and therefore this amino acid may be crucial for TagE activity (for example, active site located).…”

Section: Discussionmentioning

confidence: 99%

Repeated triggering of sporulation in Bacillus subtilis selects against a protein that affects the timing of cell division

et al. 2013

View full text Add to dashboard Cite

Bacillus subtilis sporulation is a last-resort phenotypical adaptation in response to starvation. The regulatory network underlying this developmental pathway has been studied extensively. However, how sporulation initiation is concerted in relation to the environmental nutrient availability is poorly understood. In a fed-batch fermentation set-up, in which sporulation of ultraviolet (UV)-mutagenized B. subtilis is repeatedly triggered by periods of starvation, fitter strains with mutated tagE evolved. These mutants display altered timing of phenotypical differentiation. The substrate for the wall teichoic acid (WTA)-modifying enzyme TagE, UDP-glucose, has recently been shown to be an intracellular proxy for nutrient availability, and influences the timing of cell division. Here we suggest that UDP-glucose also influences timing of cellular differentiation.

show abstract

Section: Discussionmentioning

confidence: 99%

Repeated triggering of sporulation in Bacillus subtilis selects against a protein that affects the timing of cell division

et al. 2013

View full text Add to dashboard Cite

show abstract

“…However, the predicted secondary structure of the PvdA N-terminal region consists of a short bsheet (from H 11 to V 16 ) and an a-helix (from S 21 to Q 30 ) separated by two residues generally involved in a-helical breaking (G 19 and P 20 ). P and G residues are widely distributed in TM domains of many integral membrane proteins (Williams & Deber, 1991;Landolt-Marticorena et al, 1993), and their helical propensity is greatly enhanced in lipid bilayers (Li et al, 1996;Deber et al, 1999). Nevertheless, the N-terminal hydrophobic region of PvdA overlaps the putative FAD-binding motif.…”

Section: Discussionmentioning

confidence: 99%

Membrane-association determinants of the ω-amino acid monooxygenase PvdA, a pyoverdine biosynthetic enzyme from Pseudomonas aeruginosa

et al. 2008

View full text Add to dashboard Cite

The L-ornithine N d -oxygenase PvdA catalyses the N d -hydroxylation of L-ornithine in many Pseudomonas spp., and thus provides an essential enzymic function in the biogenesis of the pyoverdine siderophore. Here, we report a detailed analysis of the membrane topology of the PvdA enzyme from the bacterial pathogen Pseudomonas aeruginosa. Membrane topogenic determinants of PvdA were identified by computational analysis, and verified in Escherichia coli by constructing a series of translational fusions between PvdA and the PhoA (alkaline phosphatase) reporter enzyme. The inferred topological model resembled a eukaryotic reverse signal-anchor (type III) protein, with a single N-terminal domain anchored to the inner membrane, and the bulk of the protein spanning the cytosol. According to this model, the predicted transmembrane region should overlap the putative FAD-binding site. Cell fractionation and proteinase K accessibility experiments in P. aeruginosa confirmed the membrane-bound nature of PvdA, but excluded the transmembrane topology of its N-terminal hydrophobic region. Mutational analysis of PvdA, and complementation assays in a P. aeruginosa DpvdA mutant, demonstrated the dual (structural and functional) role of the PvdA N-terminal domain.

show abstract

“…Prolines have one fixed dihedral angle and segments containing proline generally have increased rigidity and can provide a focus for protein folding and assembly (29,30). This residue is often present in turns and is not averse to being exposed to water.…”

Section: Discussionmentioning

confidence: 99%

The Polymorphism P315L of Human Toll-Like Receptor 1 Impairs Innate Immune Sensing of Microbial Cell Wall Components

Omueti

Mazur²,

Thompson³

et al. 2007

The Journal of Immunology

View full text Add to dashboard Cite

As a pattern recognition receptor, TLR1 mediates innate immune responses to a variety of microbial cell wall components including bacterial lipoproteins. We have previously shown that the central region of the extracellular domain of human TLR1, comprising leucine-rich repeat (LRR) motifs 9–12, is required for the sensing of bacterial lipopeptides. In this study, we have investigated three nonsynonymous single nucleotide polymorphisms (SNPs) located in this region of TLR1 by generating these variants and examining receptor function. We have found that a variant of TLR1 based upon the SNP P315L, located in the loop of LRR motif 11 (LRR11), is greatly impaired in mediating responses to lipopeptides and a variety of other bacterial agonists for this receptor. Despite normal cell surface expression, the P315L variant also fails to bind to GD2.F4, a commonly used anti-TLR1 mAb. Although a number of amino acid substitutions at position 315 impair receptor function, the leucine substitution has the strongest deleterious effect. GD2.F4 inhibits agonist-induced activation of TLR1, supporting a crucial role for the loop of LRR11 in receptor function. These results also suggest that the P315L SNP may predispose certain individuals to infectious diseases for which the sensing of microbial cell components by TLR1 is critical to innate immune defense.

show abstract

Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment.

Abstract: Proline is established as a potent breaker of both et-helical and 13-sheet structures in soluble (globular) proteins.

Cited by 285 publications

References 54 publications

Repeated triggering of sporulation in Bacillus subtilis selects against a protein that affects the timing of cell division

Repeated triggering of sporulation in Bacillus subtilis selects against a protein that affects the timing of cell division

Membrane-association determinants of the ω-amino acid monooxygenase PvdA, a pyoverdine biosynthetic enzyme from Pseudomonas aeruginosa

The Polymorphism P315L of Human Toll-Like Receptor 1 Impairs Innate Immune Sensing of Microbial Cell Wall Components

Contact Info

Product

Resources

About