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  • Valegård, KarinUppsala universitet,Institutionen för cell- och molekylärbiologi (author)

Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications

  • Article/chapterEnglish2018

Publisher, publication year, extent ...

  • 2018
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:uu-364046
  • https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-364046URI
  • https://doi.org/10.1074/jbc.RA118.003518DOI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • The catalytic performance of the major CO2-assimilating enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), restricts photosynthetic productivity. Natural diversity in the catalytic properties of Rubisco indicates possibilities for improvement. Oceanic phytoplankton contain some of the most efficient Rubisco enzymes, and diatoms in particular are responsible for a significant proportion of total marine primary production as well as being a major source of CO2 sequestration in polar cold waters. Until now, the biochemical properties and three-dimensional structures of Rubisco from diatoms were unknown. Here, diatoms from arctic waters were collected, cultivated, and analyzed for their CO2-fixing capability. We characterized the kinetic properties of five and determined the crystal structures of four Rubiscos selected for their high CO2-fixing efficiency. The DNA sequences of the rbcL, and rbcS genes of the selected diatoms were similar, reflecting their close phylogenetic relationship. The V-max and K-m for the oxygenase and carboxylase activities at 25 degrees C and the specificity factors (S-c/o) at 15, 25, and 35 degrees C were determined. The S-c/o values were high, approaching those of mono- and dicot plants, thus exhibiting good selectivity for CO(2 )relative to O-2. Structurally, diatom Rubiscos belong to form I C/D, containing small subunits characterized by a short beta A-beta B loop and a C-terminal extension that forms a beta-hairpin structure (beta E-beta F loop). Of note, the diatom Rubiscos featured a number of posttranslational modifications of the large subunit, including 4-hydroxyproline, beta-hydroxyleucine, hydroxylated and nitrosylated cysteine, mono- and dihydroxylated lysine, and trimethylated lysine. Our studies suggest adaptation toward achieving efficient CO2 fixation in arctic diatom Rubiscos.

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  • Andralojc, P. JohnRothamsted Res, Dept Plant Sci, Harpenden AL5 2JQ, Herts, England (author)
  • Haslam, Richard P.Rothamsted Res, Dept Plant Sci, Harpenden AL5 2JQ, Herts, England (author)
  • Pearce, F. GrantUppsala universitet,Institutionen för cell- och molekylärbiologi,Univ Canterbury, Sch Biol Sci, Private Bag 4800, Christchurch 8140, New Zealand (author)
  • Eriksen, Gunilla K.Arctic Univ Norway, Norwegian Coll Fisheries Sci, N-9037 Tromso, Norway (author)
  • Madgwickn, Pippa J.Rothamsted Res, Dept Plant Sci, Harpenden AL5 2JQ, Herts, England (author)
  • Kristoffersen, Anne K.Univ Oslo, Dept Biosci, POB 1066, N-0316 Oslo, Norway;Univ Oslo, Fac Dent, Dept Oral Biol, POB 1052, N-0316 Oslo, Norway (author)
  • van Lun, MichielUppsala universitet,Institutionen för cell- och molekylärbiologi(Swepub:uu)milun205 (author)
  • Klein, UweUniv Oslo, Dept Biosci, POB 1066, N-0316 Oslo, Norway (author)
  • Eilertsen, Hans C.Arctic Univ Norway, Norwegian Coll Fisheries Sci, N-9037 Tromso, Norway (author)
  • Parry, Martin A. J.Rothamsted Res, Dept Plant Sci, Harpenden AL5 2JQ, Herts, England;Univ Lancaster, Lancaster Environm Ctr, Lancaster LA1 4YQ, England (author)
  • Andersson, IngerUppsala universitet,Molekylär biofysik(Swepub:uu)inand172 (author)
  • Uppsala universitetInstitutionen för cell- och molekylärbiologi (creator_code:org_t)

Related titles

  • In:Journal of Biological Chemistry293:34, s. 13033-130430021-92581083-351X

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