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Sökning: id:"swepub:oai:DiVA.org:uu-364046" > Structural and func...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004513naa a2200409 4500
001oai:DiVA.org:uu-364046
003SwePub
008181210s2018 | |||||||||||000 ||eng|
024a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3640462 URI
024a https://doi.org/10.1074/jbc.RA118.0035182 DOI
040 a (SwePub)uu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Valegård, Karinu Uppsala universitet,Institutionen för cell- och molekylärbiologi4 aut0 (Swepub:uu)kva15730
2451 0a Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications
264 1c 2018
338 a print2 rdacarrier
520 a 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.
650 7a NATURVETENSKAPx Biologix Botanik0 (SwePub)106072 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Botany0 (SwePub)106072 hsv//eng
700a Andralojc, P. Johnu Rothamsted Res, Dept Plant Sci, Harpenden AL5 2JQ, Herts, England4 aut
700a Haslam, Richard P.u Rothamsted Res, Dept Plant Sci, Harpenden AL5 2JQ, Herts, England4 aut
700a Pearce, F. Grantu Uppsala universitet,Institutionen för cell- och molekylärbiologi,Univ Canterbury, Sch Biol Sci, Private Bag 4800, Christchurch 8140, New Zealand4 aut
700a Eriksen, Gunilla K.u Arctic Univ Norway, Norwegian Coll Fisheries Sci, N-9037 Tromso, Norway4 aut
700a Madgwickn, Pippa J.u Rothamsted Res, Dept Plant Sci, Harpenden AL5 2JQ, Herts, England4 aut
700a Kristoffersen, Anne K.u Univ Oslo, Dept Biosci, POB 1066, N-0316 Oslo, Norway;Univ Oslo, Fac Dent, Dept Oral Biol, POB 1052, N-0316 Oslo, Norway4 aut
700a van Lun, Michielu Uppsala universitet,Institutionen för cell- och molekylärbiologi4 aut0 (Swepub:uu)milun205
700a Klein, Uweu Univ Oslo, Dept Biosci, POB 1066, N-0316 Oslo, Norway4 aut
700a Eilertsen, Hans C.u Arctic Univ Norway, Norwegian Coll Fisheries Sci, N-9037 Tromso, Norway4 aut
700a Parry, Martin A. J.u Rothamsted Res, Dept Plant Sci, Harpenden AL5 2JQ, Herts, England;Univ Lancaster, Lancaster Environm Ctr, Lancaster LA1 4YQ, England4 aut
700a Andersson, Ingeru Uppsala universitet,Molekylär biofysik4 aut0 (Swepub:uu)inand172
710a Uppsala universitetb Institutionen för cell- och molekylärbiologi4 org
773t Journal of Biological Chemistryg 293:34, s. 13033-13043q 293:34<13033-13043x 0021-9258x 1083-351X
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-364046
8564 8u https://doi.org/10.1074/jbc.RA118.003518

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