PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactis.

<h4>Background</h4>Protein folding in the envelope is a crucial limiting step of protein export and secretion. In order to better understand this process in Lactococcus lactis, a lactic acid bacterium, genes encoding putative exported folding factors like Peptidyl Prolyl Isomerases (PPIa...

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Autores principales:	Nicolas Trémillon, Eric Morello, Daniel Llull, Rabia Mazmouz, Jean-Jacques Gratadoux, Alain Guillot, Marie-Pierre Chapot-Chartier, Laura Monlezun, Véronique Solé, Hervé Ginisty, Isabelle Poquet
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/288b2ea250a8421cbe12cfeeef66bf48
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spelling	oai:doaj.org-article:288b2ea250a8421cbe12cfeeef66bf482021-11-18T07:24:48ZPpiA, a surface PPIase of the cyclophilin family in Lactococcus lactis.1932-620310.1371/journal.pone.0033516https://doaj.org/article/288b2ea250a8421cbe12cfeeef66bf482012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22442694/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Protein folding in the envelope is a crucial limiting step of protein export and secretion. In order to better understand this process in Lactococcus lactis, a lactic acid bacterium, genes encoding putative exported folding factors like Peptidyl Prolyl Isomerases (PPIases) were searched for in lactococcal genomes.<h4>Results</h4>In L. lactis, a new putative membrane PPIase of the cyclophilin subfamily, PpiA, was identified and characterized. ppiA gene was found to be constitutively expressed under normal and stress (heat shock, H(2)O(2)) conditions. Under normal conditions, PpiA protein was synthesized and released from intact cells by an exogenously added protease, showing that it was exposed at the cell surface. No obvious phenotype could be associated to a ppiA mutant strain under several laboratory conditions including stress conditions, except a very low sensitivity to H(2)O(2). Induction of a ppiA copy provided in trans had no effect i) on the thermosensitivity of an mutant strain deficient for the lactococcal surface protease HtrA and ii) on the secretion and stability on four exported proteins (a highly degraded hybrid protein and three heterologous secreted proteins) in an otherwise wild-type strain background. However, a recombinant soluble form of PpiA that had been produced and secreted in L. lactis and purified from a culture supernatant displayed both PPIase and chaperone activities.<h4>Conclusions</h4>Although L. lactis PpiA, a protein produced and exposed at the cell surface under normal conditions, displayed a very moderate role in vivo, it was found, as a recombinant soluble form, to be endowed with folding activities in vitro.Nicolas TrémillonEric MorelloDaniel LlullRabia MazmouzJean-Jacques GratadouxAlain GuillotMarie-Pierre Chapot-ChartierLaura MonlezunVéronique SoléHervé GinistyIsabelle PoquetPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 3, p e33516 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nicolas Trémillon Eric Morello Daniel Llull Rabia Mazmouz Jean-Jacques Gratadoux Alain Guillot Marie-Pierre Chapot-Chartier Laura Monlezun Véronique Solé Hervé Ginisty Isabelle Poquet PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactis.
description	<h4>Background</h4>Protein folding in the envelope is a crucial limiting step of protein export and secretion. In order to better understand this process in Lactococcus lactis, a lactic acid bacterium, genes encoding putative exported folding factors like Peptidyl Prolyl Isomerases (PPIases) were searched for in lactococcal genomes.<h4>Results</h4>In L. lactis, a new putative membrane PPIase of the cyclophilin subfamily, PpiA, was identified and characterized. ppiA gene was found to be constitutively expressed under normal and stress (heat shock, H(2)O(2)) conditions. Under normal conditions, PpiA protein was synthesized and released from intact cells by an exogenously added protease, showing that it was exposed at the cell surface. No obvious phenotype could be associated to a ppiA mutant strain under several laboratory conditions including stress conditions, except a very low sensitivity to H(2)O(2). Induction of a ppiA copy provided in trans had no effect i) on the thermosensitivity of an mutant strain deficient for the lactococcal surface protease HtrA and ii) on the secretion and stability on four exported proteins (a highly degraded hybrid protein and three heterologous secreted proteins) in an otherwise wild-type strain background. However, a recombinant soluble form of PpiA that had been produced and secreted in L. lactis and purified from a culture supernatant displayed both PPIase and chaperone activities.<h4>Conclusions</h4>Although L. lactis PpiA, a protein produced and exposed at the cell surface under normal conditions, displayed a very moderate role in vivo, it was found, as a recombinant soluble form, to be endowed with folding activities in vitro.
format	article
author	Nicolas Trémillon Eric Morello Daniel Llull Rabia Mazmouz Jean-Jacques Gratadoux Alain Guillot Marie-Pierre Chapot-Chartier Laura Monlezun Véronique Solé Hervé Ginisty Isabelle Poquet
author_facet	Nicolas Trémillon Eric Morello Daniel Llull Rabia Mazmouz Jean-Jacques Gratadoux Alain Guillot Marie-Pierre Chapot-Chartier Laura Monlezun Véronique Solé Hervé Ginisty Isabelle Poquet
author_sort	Nicolas Trémillon
title	PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactis.
title_short	PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactis.
title_full	PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactis.
title_fullStr	PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactis.
title_full_unstemmed	PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactis.
title_sort	ppia, a surface ppiase of the cyclophilin family in lactococcus lactis.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/288b2ea250a8421cbe12cfeeef66bf48
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PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactis.

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