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Your search keyword '"Pugsley, Anthony P."' showing total 7 results
Start Over Author "Pugsley, Anthony P." Journal journal of biological chemistry
7 results on '"Pugsley, Anthony P."'

6. Type III Protein Translocase

Author

Pozidis, Charalambos, primary, Chalkiadaki, Aggeliki, additional, Gomez-Serrano, Amalia, additional, Stahlberg, Henning, additional, Brown, Ian, additional, Tampakaki, Anastasia P., additional, Lustig, Ariel, additional, Sianidis, Giorgos, additional, Politou, Anastasia S., additional, Engel, Andreas, additional, Panopoulos, Nickolas J., additional, Mansfield, John, additional, Pugsley, Anthony P., additional, Karamanou, Spyridoula, additional, and Economou, Anastassios, additional

Published
2003
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7. Prepore Stability Controls Productive Folding of the BAMindependent Multimeric Outer Membrane Secretin PulD.

Author

Guilvout, Ingrid, Brier, Sébastien, Chami, Mohamed, Hourdel, Véronique, Francetic, Olivera, Pugsley, Anthony P., Chamot-Rooke, Julia, and Huysmans, Gerard H. M.

Subjects
*SECRETIN, *BACTERIAL cell walls, *GRAM-negative bacteria, *DEUTERIUM, *ELECTRON microscopy
Abstract

Members of a group of multimeric secretion pores that assemble independently of any known membrane-embedded insertase in Gram-negative bacteria fold into a prepore before membrane-insertion occurs. The mechanisms and the energetics that drive the folding of these proteins are poorly understood. Here, equilibrium unfolding and hydrogen/deuterium exchange monitored by mass spectrometry indicated that a loss of 4-5 kJ/mol/protomer in the N3 domain that is peripheral to the membrane-spanning C domain in the dodecameric secretin PulD, the founding member of this class, prevents pore formation by destabilizing the prepore into a poorly structured dodecamer as visualized by electron microscopy. Formation of native PulD-multimers by mixing protomers that differ in N3 domain stability, suggested that the N3 domain forms a thermodynamic seal onto the prepore. This highlights the role of modest free energy changes in the folding of preintegration forms of a hyperstable outer membrane complex and reveals a key driving force for assembly independently of the β-barrel assembly machinery. [ABSTRACT FROM AUTHOR]

Published
2017
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