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Previous work demonstrated that a phasin from\n \n A<\/jats:italic>\n <\/jats:styled-content>\n zotobacter<\/jats:italic>\n sp\n FA<\/jats:styled-content>\n \u20108 (\n PhaP<\/jats:styled-content>\n Az<\/jats:sub>\n ) had an unexpected growth\u2010promoting and stress\u2010protecting effect in\n \n E<\/jats:italic>\n <\/jats:styled-content>\n scherichia coli<\/jats:italic>\n , suggesting it could have chaperone\u2010like activities. In this work,\n in vitro<\/jats:italic>\n and\n in vivo<\/jats:italic>\n experiments were performed in order to investigate this possibility.\n PhaP<\/jats:styled-content>\n Az<\/jats:sub>\n was shown to prevent\n in vitro<\/jats:italic>\n thermal aggregation of the model protein citrate synthase and to facilitate the refolding process of this enzyme after chemical denaturation. Microscopy techniques were used to analyse the subcellular localization of\n PhaP<\/jats:styled-content>\n Az<\/jats:sub>\n in\n \n E<\/jats:italic>\n <\/jats:styled-content>\n .\u2009coli<\/jats:italic>\n strains and to study the role of\n PhaP<\/jats:styled-content>\n Az<\/jats:sub>\n in\n in vivo<\/jats:italic>\n protein folding and aggregation.\n PhaP<\/jats:styled-content>\n Az<\/jats:sub>\n was shown to colocalize with inclusion bodies of\n PD<\/jats:styled-content>\n , a protein that aggregates when overexpressed. A reduction in the number of inclusion bodies of\n PD<\/jats:styled-content>\n was observed when it was coexpressed with\n PhaP<\/jats:styled-content>\n Az<\/jats:sub>\n or with the known chaperone\n GroELS<\/jats:styled-content>\n . These results demonstrate that\n PhaP<\/jats:styled-content>\n Az<\/jats:sub>\n has chaperone\u2010like functions both\n in vitro<\/jats:italic>\n and\n in vivo<\/jats:italic>\n in\n \n E<\/jats:italic>\n <\/jats:styled-content>\n .\u2009coli<\/jats:italic>\n recombinants, and suggests that phasins could have a general protective role in natural polyhydroxyalkanoate producers.\n <\/jats:p>","DOI":"10.1111\/1462-2920.12636","type":"journal-article","created":{"date-parts":[[2014,10,8]],"date-time":"2014-10-08T23:27:20Z","timestamp":1412810840000},"page":"1765-1776","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":38,"title":["A phasin with extra talents: a polyhydroxyalkanoate granule\u2010associated protein has chaperone activity"],"prefix":"10.1111","volume":"17","author":[{"given":"Mariela P.","family":"Mezzina","sequence":"first","affiliation":[{"name":"Departamento de Qu\u00edmica Biol\u00f3gica Facultad de Ciencias Exactas y Naturales Universidad de Buenos Aires, IQUIBICEN\u2010CONICET Buenos Aires Argentina"}]},{"given":"Diana E.","family":"Wetzler","sequence":"additional","affiliation":[{"name":"Departamento de Qu\u00edmica Biol\u00f3gica Facultad de Ciencias Exactas y Naturales Universidad de Buenos Aires, IQUIBICEN\u2010CONICET Buenos Aires Argentina"}]},{"given":"Alejandra","family":"de Almeida","sequence":"additional","affiliation":[{"name":"Departamento de Qu\u00edmica Biol\u00f3gica Facultad de Ciencias Exactas y Naturales Universidad de Buenos Aires, IQUIBICEN\u2010CONICET Buenos Aires Argentina"}]},{"given":"Nina","family":"Dinjaski","sequence":"additional","affiliation":[{"name":"Centro de Investigaciones Biol\u00f3gicas Consejo Superior de Investigaciones Cient\u00edficas Madrid Spain"}]},{"given":"M. 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