Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis.

The bacterial second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP) has emerged as a central regulator for biofilm formation. Increased cellular c-di-GMP levels lead to stable cell attachment, which in Pseudomonas fluorescens requires the transmembrane receptor Lap...

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Autores principales:	Marcos V A S Navarro, Peter D Newell, Petya V Krasteva, Debashree Chatterjee, Dean R Madden, George A O'Toole, Holger Sondermann
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/b8ea3abfdd0b44f98ffdfe8b6f275a74
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spelling	oai:doaj.org-article:b8ea3abfdd0b44f98ffdfe8b6f275a742021-11-18T05:36:20ZStructural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis.1544-91731545-788510.1371/journal.pbio.1000588https://doaj.org/article/b8ea3abfdd0b44f98ffdfe8b6f275a742011-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21304926/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885The bacterial second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP) has emerged as a central regulator for biofilm formation. Increased cellular c-di-GMP levels lead to stable cell attachment, which in Pseudomonas fluorescens requires the transmembrane receptor LapD. LapD exhibits a conserved and widely used modular architecture containing a HAMP domain and degenerate diguanylate cyclase and phosphodiesterase domains. c-di-GMP binding to the LapD degenerate phosphodiesterase domain is communicated via the HAMP relay to the periplasmic domain, triggering sequestration of the protease LapG, thus preventing cleavage of the surface adhesin LapA. Here, we elucidate the molecular mechanism of autoinhibition and activation of LapD based on structure-function analyses and crystal structures of the entire periplasmic domain and the intracellular signaling unit in two different states. In the absence of c-di-GMP, the intracellular module assumes an inactive conformation. Binding of c-di-GMP to the phosphodiesterase domain disrupts the inactive state, permitting the formation of a trans-subunit dimer interface between adjacent phosphodiesterase domains via interactions conserved in c-di-GMP-degrading enzymes. Efficient mechanical coupling of the conformational changes across the membrane is realized through an extensively domain-swapped, unique periplasmic fold. Our structural and functional analyses identified a conserved system for the regulation of periplasmic proteases in a wide variety of bacteria, including many free-living and pathogenic species.Marcos V A S NavarroPeter D NewellPetya V KrastevaDebashree ChatterjeeDean R MaddenGeorge A O'TooleHolger SondermannPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 9, Iss 2, p e1000588 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Marcos V A S Navarro Peter D Newell Petya V Krasteva Debashree Chatterjee Dean R Madden George A O'Toole Holger Sondermann Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis.
description	The bacterial second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP) has emerged as a central regulator for biofilm formation. Increased cellular c-di-GMP levels lead to stable cell attachment, which in Pseudomonas fluorescens requires the transmembrane receptor LapD. LapD exhibits a conserved and widely used modular architecture containing a HAMP domain and degenerate diguanylate cyclase and phosphodiesterase domains. c-di-GMP binding to the LapD degenerate phosphodiesterase domain is communicated via the HAMP relay to the periplasmic domain, triggering sequestration of the protease LapG, thus preventing cleavage of the surface adhesin LapA. Here, we elucidate the molecular mechanism of autoinhibition and activation of LapD based on structure-function analyses and crystal structures of the entire periplasmic domain and the intracellular signaling unit in two different states. In the absence of c-di-GMP, the intracellular module assumes an inactive conformation. Binding of c-di-GMP to the phosphodiesterase domain disrupts the inactive state, permitting the formation of a trans-subunit dimer interface between adjacent phosphodiesterase domains via interactions conserved in c-di-GMP-degrading enzymes. Efficient mechanical coupling of the conformational changes across the membrane is realized through an extensively domain-swapped, unique periplasmic fold. Our structural and functional analyses identified a conserved system for the regulation of periplasmic proteases in a wide variety of bacteria, including many free-living and pathogenic species.
format	article
author	Marcos V A S Navarro Peter D Newell Petya V Krasteva Debashree Chatterjee Dean R Madden George A O'Toole Holger Sondermann
author_facet	Marcos V A S Navarro Peter D Newell Petya V Krasteva Debashree Chatterjee Dean R Madden George A O'Toole Holger Sondermann
author_sort	Marcos V A S Navarro
title	Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis.
title_short	Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis.
title_full	Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis.
title_fullStr	Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis.
title_full_unstemmed	Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis.
title_sort	structural basis for c-di-gmp-mediated inside-out signaling controlling periplasmic proteolysis.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/b8ea3abfdd0b44f98ffdfe8b6f275a74
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Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis.

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