Surveying the expanding prokaryotic Rubisco multiverse. Issue 16 (20th July 2017)
- Record Type:
- Journal Article
- Title:
- Surveying the expanding prokaryotic Rubisco multiverse. Issue 16 (20th July 2017)
- Main Title:
- Surveying the expanding prokaryotic Rubisco multiverse
- Authors:
- Liu, Di
Ramya, Ramaswamy Chettiyan Seetharaman
Mueller-Cajar, Oliver - Abstract:
- Abstract: The universal, but catalytically modest, CO2 -fixing enzyme Rubisco is currently experiencing intense interest by researchers aiming to enhance crop photosynthesis. These efforts are mostly focused on the highly conserved hexadecameric enzyme found in land plants. In comparison, prokaryotic organisms harbor a far greater diversity in Rubisco forms. Recent work towards improving our appreciation of microbial Rubisco properties and harnessing their potential is surveyed. New structural models are providing informative glimpses into catalytic subtleties and diverse oligomeric states. Ongoing characterization is informing us about the conservation of constraints, such as sugar phosphate inhibition and the associated dependence on Rubisco activase helper proteins. Prokaryotic Rubiscos operate under a far wider range of metabolic contexts than the photosynthetic function of higher plant enzymes. Relaxed selection pressures may have resulted in the exploration of a larger volume of sequence space than permitted in organisms performing oxygenic photosynthesis. To tap into the potential of microbial Rubiscos, in vivo selection systems are being used to discover functional metagenomic Rubiscos. Various directed evolution systems to optimize their function have been developed. It is anticipated that this approach will provide access to biotechnologically valuable enzymes that cannot be encountered in the higher plant Rubisco space. Abstract : The vast majority of RubiscoAbstract: The universal, but catalytically modest, CO2 -fixing enzyme Rubisco is currently experiencing intense interest by researchers aiming to enhance crop photosynthesis. These efforts are mostly focused on the highly conserved hexadecameric enzyme found in land plants. In comparison, prokaryotic organisms harbor a far greater diversity in Rubisco forms. Recent work towards improving our appreciation of microbial Rubisco properties and harnessing their potential is surveyed. New structural models are providing informative glimpses into catalytic subtleties and diverse oligomeric states. Ongoing characterization is informing us about the conservation of constraints, such as sugar phosphate inhibition and the associated dependence on Rubisco activase helper proteins. Prokaryotic Rubiscos operate under a far wider range of metabolic contexts than the photosynthetic function of higher plant enzymes. Relaxed selection pressures may have resulted in the exploration of a larger volume of sequence space than permitted in organisms performing oxygenic photosynthesis. To tap into the potential of microbial Rubiscos, in vivo selection systems are being used to discover functional metagenomic Rubiscos. Various directed evolution systems to optimize their function have been developed. It is anticipated that this approach will provide access to biotechnologically valuable enzymes that cannot be encountered in the higher plant Rubisco space. Abstract : The vast majority of Rubisco sequences are of prokaryotic origin providing abundant opportunities for bioengineers. … (more)
- Is Part Of:
- FEMS microbiology letters. Volume 364:Issue 16(2017)
- Journal:
- FEMS microbiology letters
- Issue:
- Volume 364:Issue 16(2017)
- Issue Display:
- Volume 364, Issue 16 (2017)
- Year:
- 2017
- Volume:
- 364
- Issue:
- 16
- Issue Sort Value:
- 2017-0364-0016-0000
- Page Start:
- Page End:
- Publication Date:
- 2017-07-20
- Subjects:
- Rubisco -- CO2 fixation -- photosynthesis -- Rubisco activases -- directed evolution
Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1574-6968/issues ↗
http://www.sciencedirect.com/science/journal/03781097 ↗
http://onlinelibrary.wiley.com/ ↗
http://femsle.oxfordjournals.org/content/ ↗
http://firstsearch.oclc.org ↗ - DOI:
- 10.1093/femsle/fnx156 ↗
- Languages:
- English
- ISSNs:
- 0378-1097
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.300000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 25646.xml