Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis

Protein Science : a Publication of the Protein Society
Megan R WimmerTodd M Weaver

Abstract

Protein secretion is a major contributor to Gram-negative bacterial virulence. Type Vb or two-partner secretion (TPS) pathways utilize a membrane bound β-barrel B component (TpsB) to translocate large and predominantly virulent exoproteins (TpsA) through a nucleotide independent mechanism. We focused our studies on a truncated TpsA member termed hemolysin A (HpmA265), a structurally and functionally characterized TPS domain from Proteus mirabilis. Contrary to the expectation that the TPS domain of HpmA265 would denature in a single cooperative transition, we found that the unfolding follows a sequential model with three distinct transitions linking four states. The solvent inaccessible core of HpmA265 can be divided into two different regions. The C-proximal region contains nonpolar residues and forms a prototypical hydrophobic core as found in globular proteins. The N-proximal region of the solvent inaccessible core, however, contains polar residues. To understand the contributions of the hydrophobic and polar interiors to overall TPS domain stability, we conducted unfolding studies on HpmA265 and site-specific mutants of HpmA265. By correlating the effect of individual site-specific mutations with the sequential unfolding res...Continue Reading

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Citations

Mar 16, 2017·Acta Crystallographica. Section F, Structural Biology Communications·Walter R P NovakTodd M Weaver
Sep 13, 2019·Protein Science : a Publication of the Protein Society·Megan R WimmerTodd M Weaver
May 26, 2017·Frontiers in Cellular and Infection Microbiology·Jeremy GuérinFrançoise Jacob-Dubuisson
Feb 10, 2018·EcoSal Plus·Chelsie E ArmbrusterMelanie M Pearson

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