The Hidden Face of Rubisco. (May 2018)
- Record Type:
- Journal Article
- Title:
- The Hidden Face of Rubisco. (May 2018)
- Main Title:
- The Hidden Face of Rubisco
- Authors:
- Pottier, Mathieu
Gilis, Dimitri
Boutry, Marc - Abstract:
- Abstract : R ibu lose-1, 5-bis phosphate c arboxylase/o xygenase (Rubisco) fixes atmospheric CO2 into organic compounds and is composed of eight copies each of a large subunit (RbcL) and a small subunit (RbcS). Recent reports have revealed unusual RbcS, which are expressed in particular tissues and confer higher catalytic rate, lesser affinity for CO2, and a more acidic profile of the activity versus pH. The resulting Rubisco was proposed to be adapted to a high CO2 environment and recycle CO2 generated by the metabolism. These RbcS belong to a cluster named T (for trichome), phylogenetically distant from cluster M, which gathers well-characterized RbcS expressed in mesophyll or bundle-sheath tissues. Cluster T is largely represented in different plant phyla, including pteridophytes and bryophytes, indicating an ancient origin. Highlights: R ibu lose-1, 5-bis phosphate c arboxylase/o xygenase (Rubisco) is a highly abundant chloroplast enzyme that fixes atmospheric CO2 into organic compounds. It is composed of eight copies of a large subunit (RbcL) and eight copies of a small subunit (RbcS). Genes that encode a particular RbcS (named RbcS-T) have been recently discovered in several species from different plant phyla. They are phylogenetically distant from well-characterized genes encoding RbcS (named RbcS-M), which are typically expressed in mesophyll and bundle sheaths. Biochemical characterization of RbcS-T-containing Rubisco has revealed higher catalytic activity, higherAbstract : R ibu lose-1, 5-bis phosphate c arboxylase/o xygenase (Rubisco) fixes atmospheric CO2 into organic compounds and is composed of eight copies each of a large subunit (RbcL) and a small subunit (RbcS). Recent reports have revealed unusual RbcS, which are expressed in particular tissues and confer higher catalytic rate, lesser affinity for CO2, and a more acidic profile of the activity versus pH. The resulting Rubisco was proposed to be adapted to a high CO2 environment and recycle CO2 generated by the metabolism. These RbcS belong to a cluster named T (for trichome), phylogenetically distant from cluster M, which gathers well-characterized RbcS expressed in mesophyll or bundle-sheath tissues. Cluster T is largely represented in different plant phyla, including pteridophytes and bryophytes, indicating an ancient origin. Highlights: R ibu lose-1, 5-bis phosphate c arboxylase/o xygenase (Rubisco) is a highly abundant chloroplast enzyme that fixes atmospheric CO2 into organic compounds. It is composed of eight copies of a large subunit (RbcL) and eight copies of a small subunit (RbcS). Genes that encode a particular RbcS (named RbcS-T) have been recently discovered in several species from different plant phyla. They are phylogenetically distant from well-characterized genes encoding RbcS (named RbcS-M), which are typically expressed in mesophyll and bundle sheaths. Biochemical characterization of RbcS-T-containing Rubisco has revealed higher catalytic activity, higher Km for CO2, and an acidic shift of the activity versus pH profile. … (more)
- Is Part Of:
- Trends in plant science. Volume 23:Number 5(2018)
- Journal:
- Trends in plant science
- Issue:
- Volume 23:Number 5(2018)
- Issue Display:
- Volume 23, Issue 5 (2018)
- Year:
- 2018
- Volume:
- 23
- Issue:
- 5
- Issue Sort Value:
- 2018-0023-0005-0000
- Page Start:
- 382
- Page End:
- 392
- Publication Date:
- 2018-05
- Subjects:
- CO2 recycling -- evolution -- photosynthesis -- RbcS -- trichome -- structure
Botany -- Periodicals
Botanique -- Périodiques
Botany
Periodicals
580.5 - Journal URLs:
- http://www.sciencedirect.com/science/journal/13601385 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.tplants.2018.02.006 ↗
- Languages:
- English
- ISSNs:
- 1360-1385
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 9049.675450
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 20950.xml