Solvation driven conformational transitions in the second transmembrane domain of mycobacteriophage holin. Issue 1 (January 2017)

• Record Type: Journal Article
• Authors: Lella, Muralikrishna; Mahalakshmi, Radhakrishnan
• Other Names: Toniolo Claudio guestEditor.; Ganesh Krishna guestEditor.; Gopi Hosahudya guestEditor.; Balaram P. guestEditor.
• Is Part Of: Biopolymers. Volume 108:Issue 1(2017)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2017-01
• Subjects: Mycobacteriophage holin -- peptide helices -- circular dichroism spectroscopy -- transmembrane peptide -- polyproline II structure; Biopolymers -- Periodicals; Peptides -- Periodicals; Spectrum analysis -- Periodicals; 572.33
• DOI: 10.1002/bip.22894
• Languages: English
• ISSNs: 0006-3525

Abstract

ABSTRACT: Holins are pore‐forming membrane proteins synthesized by lytic phages. The second transmembrane domain (TM2) of Mycobacteriophage D29 holin presents an Ala‐ and Gly‐rich sequence, with a currently unknown structure and function. In this study, we present the spectroscopic characterization of synthetic TM2 in various solvents, detergents, and lipids. We find that TM2 adopts α‐helical conformation under conditions that promote intra‐strand hydrogen bonding, such as organic solvents and detergent micelles. When we transfer the peptide to a well‐hydrated environment, a polyproline II‐like structure is obtained. Surprisingly, we find that the polyproline II–like conformation is retained in lipid vesicles. Based on our results, we present a putative role for TM2 in the process of pore formation by holin. © 2016 The Authors. Peptide Science Published by Wiley Periodicals, Inc. Biopolymers (Pept Sci) 108: 1–10, 2017.