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Enhanced growth at low light intensity in the cyanobacterium Synechocystis PCC 6803 by overexpressing phosphoenolpyruvate carboxylase
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics. Hasanuddin Univ, Fac Marine Sci & Fisheries, Jl Perintis Kemerdekaan Km 10, Makassar, South Sulawesi, Indonesia..
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
2016 (English)In: ALGAL RESEARCH-BIOMASS BIOFUELS AND BIOPRODUCTS, ISSN 2211-9264, Vol. 16, 275-281 p.Article in journal (Refereed) PublishedText
Abstract [en]

Synechocystis PCC 6803 strains overexpressing pepc, gene encoding the carbon fixing enzyme phosphoenolpyruvate carboxylase (PEPc), were constructed and characterized for growth, PEPc protein content and in vitro PEPc activities. Synechocystis strains WT + Km(r) - one (native) copy of pepc (control), WT + 2xPEPc - native copy of pepc and two additional native copies of pepc (in total three copies of pepc), and WT + PPM - native copies of ppsa (encoding phosphoenolpyruvate synthase), pepc and mdh (encoding malate dehydrogenase) and one additional copy of each gene (in total two copies each of ppsa, pepc and mdh) were analyzed for growth under normal and low light intensities, and in darkness (no growth). No significant differences in the growth rates were observed when the cells were grown under normal light intensity. However, growth under low light intensity (3 mu mol photons.m(-2).sec(-1)) resulted in increased growth rate, in particular in the strain with 3 copies of pepc. SDS-PAGE/Western immunoblots using antibodies directed against PEPc demonstrated an increased level of PEPc protein with increasing number of copies of pepc. This was followed by increased levels of in vitro PEPc activities. A less efficient ribulose 1,5-bisphosphate carboxylase/oxygenase in combination with reduced levels of NADPH and ATP under low light condition may make the relatively more efficient carbon fixing enzyme PEPc the limiting step for growth under this condition.

Place, publisher, year, edition, pages
2016. Vol. 16, 275-281 p.
Keyword [en]
Genetic engineering, Enhanced growth, pepc, Phosphoenolpyruvate carboxylase, Synechocystis
National Category
Bio Materials
Identifiers
URN: urn:nbn:se:uu:diva-297764DOI: 10.1016/j.algal.2016.03.027ISI: 000375610000032OAI: oai:DiVA.org:uu-297764DiVA: diva2:943679
Funder
Knut and Alice Wallenberg Foundation, 2011.0067Swedish Energy Agency
Available from: 2016-06-28 Created: 2016-06-28 Last updated: 2016-06-28Bibliographically approved

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Durall de la Fuente, ClaudiaLindblad, Peter
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