Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis.

Metabolic control of gene expression coordinates the levels of specific gene products to meet cellular demand for their activities. This control can be exerted by metabolites acting as regulatory signals and/or a class of metabolic enzymes with dual functions as regulators of gene expression. Howeve...

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Autores principales:	Alexandra-Viola Bohne, Christian Schwarz, Marco Schottkowski, Michael Lidschreiber, Markus Piotrowski, William Zerges, Jörg Nickelsen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/5f216a7276b04e6f824fde8327e40078
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spelling	oai:doaj.org-article:5f216a7276b04e6f824fde8327e400782021-11-18T05:37:15ZReciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis.1544-91731545-788510.1371/journal.pbio.1001482https://doaj.org/article/5f216a7276b04e6f824fde8327e400782013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23424285/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Metabolic control of gene expression coordinates the levels of specific gene products to meet cellular demand for their activities. This control can be exerted by metabolites acting as regulatory signals and/or a class of metabolic enzymes with dual functions as regulators of gene expression. However, little is known about how metabolic signals affect the balance between enzymatic and regulatory roles of these dual functional proteins. We previously described the RNA binding activity of a 63 kDa chloroplast protein from Chlamydomonas reinhardtii, which has been implicated in expression of the psbA mRNA, encoding the D1 protein of photosystem II. Here, we identify this factor as dihydrolipoamide acetyltransferase (DLA2), a subunit of the chloroplast pyruvate dehydrogenase complex (cpPDC), which is known to provide acetyl-CoA for fatty acid synthesis. Analyses of RNAi lines revealed that DLA2 is involved in the synthesis of both D1 and acetyl-CoA. Gel filtration analyses demonstrated an RNP complex containing DLA2 and the chloroplast psbA mRNA specifically in cells metabolizing acetate. An intrinsic RNA binding activity of DLA2 was confirmed by in vitro RNA binding assays. Results of fluorescence microscopy and subcellular fractionation experiments support a role of DLA2 in acetate-dependent localization of the psbA mRNA to a translation zone within the chloroplast. Reciprocally, the activity of the cpPDC was specifically affected by binding of psbA mRNA. Beyond that, in silico analysis and in vitro RNA binding studies using recombinant proteins support the possibility that RNA binding is an ancient feature of dihydrolipoamide acetyltransferases. Our results suggest a regulatory function of DLA2 in response to growth on reduced carbon energy sources. This raises the intriguing possibility that this regulation functions to coordinate the synthesis of lipids and proteins for the biogenesis of photosynthetic membranes.Alexandra-Viola BohneChristian SchwarzMarco SchottkowskiMichael LidschreiberMarkus PiotrowskiWilliam ZergesJörg NickelsenPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 11, Iss 2, p e1001482 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Alexandra-Viola Bohne Christian Schwarz Marco Schottkowski Michael Lidschreiber Markus Piotrowski William Zerges Jörg Nickelsen Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis.
description	Metabolic control of gene expression coordinates the levels of specific gene products to meet cellular demand for their activities. This control can be exerted by metabolites acting as regulatory signals and/or a class of metabolic enzymes with dual functions as regulators of gene expression. However, little is known about how metabolic signals affect the balance between enzymatic and regulatory roles of these dual functional proteins. We previously described the RNA binding activity of a 63 kDa chloroplast protein from Chlamydomonas reinhardtii, which has been implicated in expression of the psbA mRNA, encoding the D1 protein of photosystem II. Here, we identify this factor as dihydrolipoamide acetyltransferase (DLA2), a subunit of the chloroplast pyruvate dehydrogenase complex (cpPDC), which is known to provide acetyl-CoA for fatty acid synthesis. Analyses of RNAi lines revealed that DLA2 is involved in the synthesis of both D1 and acetyl-CoA. Gel filtration analyses demonstrated an RNP complex containing DLA2 and the chloroplast psbA mRNA specifically in cells metabolizing acetate. An intrinsic RNA binding activity of DLA2 was confirmed by in vitro RNA binding assays. Results of fluorescence microscopy and subcellular fractionation experiments support a role of DLA2 in acetate-dependent localization of the psbA mRNA to a translation zone within the chloroplast. Reciprocally, the activity of the cpPDC was specifically affected by binding of psbA mRNA. Beyond that, in silico analysis and in vitro RNA binding studies using recombinant proteins support the possibility that RNA binding is an ancient feature of dihydrolipoamide acetyltransferases. Our results suggest a regulatory function of DLA2 in response to growth on reduced carbon energy sources. This raises the intriguing possibility that this regulation functions to coordinate the synthesis of lipids and proteins for the biogenesis of photosynthetic membranes.
format	article
author	Alexandra-Viola Bohne Christian Schwarz Marco Schottkowski Michael Lidschreiber Markus Piotrowski William Zerges Jörg Nickelsen
author_facet	Alexandra-Viola Bohne Christian Schwarz Marco Schottkowski Michael Lidschreiber Markus Piotrowski William Zerges Jörg Nickelsen
author_sort	Alexandra-Viola Bohne
title	Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis.
title_short	Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis.
title_full	Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis.
title_fullStr	Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis.
title_full_unstemmed	Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis.
title_sort	reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/5f216a7276b04e6f824fde8327e40078
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Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis.

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