نتایج جستجو برای: ribulose bisphosphate carboxylaseoxygenase activase

تعداد نتایج: 7279  

2016
Ranjeet R. Kumar Suneha Goswami Khushboo Singh Kavita Dubey Shweta Singh Renu Sharma Neeraj Verma Yugal K. Kala Gyanendra K. Rai Monendra Grover Dwijesh C. Mishra Bhupinder Singh Himanshu Pathak Viswanathan Chinnusamy Anil Rai Shelly Praveen

RuBisCo activase (Rca) is a catalytic chaperone involved in modulating the activity of RuBisCo (key enzyme of photosynthetic pathway). Here, we identified eight novel transcripts from wheat through data mining predicted to be Rca and cloned a transcript of 1.4 kb from cv. HD2985, named as TaRca1 (GenBank acc. no. KC776912). Single copy number of TaRca1 was observed in wheat genome. Expression a...

Journal: :Plant physiology 1995
G. T. Byrd D. R. Ort W. L. Ogren

Photosynthesis rate, ribulsoe-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activation state, and ribulose bisphosphate concentration were reduced after exposing tomato (Lycopersicon esculentum Mill.) plants to light at 4[deg]C for 6 h. Analysis of lysed and reconsituted chloroplasts showed that activity of the thylakoid membrane was inhibited and that Rubisco, Rubisco activase, and other so...

2015
Yue Chen Xiao-Man Wang Li Zhou Yi He Dun Wang Yan-Hua Qi De-An Jiang Niranjan Baisakh

Ribulose-1,5-bisphosphate carboxylase/oxygenase activase (RCA) is a nuclear gene that encodes a chloroplast protein that plays an important role in photosynthesis. Some reports have indicated that it may play a role in acclimation to different abiotic stresses. In this paper, we analyzed the stress-responsive elements in the 2.0 kb 5'-upstream regions of the RCA gene promoter and the primary, s...

Journal: :Journal of experimental botany 2009
Zoran Ristic Ivana Momcilovic Urska Bukovnik P V Vara Prasad Jianming Fu Benjamin P Deridder Thomas E Elthon Novica Mladenov

Rubisco activase (RCA) constrains the photosynthetic potential of plants at high temperatures (heat stress). Endogenous levels of RCA could serve as an important determinant of plant productivity under heat-stress conditions. Thus, in this study, the possible relationship between expression levels of RCA and plant yield in 11 European cultivars of winter wheat following prolonged exposure to he...

Journal: :Journal of experimental botany 2006
Michael E Salvucci Benjamin P DeRidder Archie R Portis

Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) activation decreases under moderate heat stress. This decrease is caused by an impairment of activase function, which is exacerbated by faster rates of Rubisco deactivation at elevated temperatures. To determine if stromal oxidation causes inhibition of activase, transgenic Arabidopsis plants expressing suboptimal amounts of either the r...

Journal: :Plant physiology 2000
S A Ruuska T J Andrews M R Badger G D Price S von Caemmerer

Leaf metabolites, adenylates, and Rubisco activation were studied in two transgenic tobacco (Nicotiana tabacum L. cv W38) types. Plants with reduced amounts of cytochrome b/f complex (anti-b/f) have impaired electron transport and a low transthylakoid pH gradient that restrict ATP and NADPH synthesis. Plants with reduced glyceraldehyde 3-phosphate dehydrogenase (anti-GAPDH) have a decreased cap...

Journal: :Plant physiology 1992
J B Shen W L Ogren

Site-directed mutagenesis was performed on the 1.6 and 1.9 kilobase spinach (Spinacea oleracea) ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase cDNAs, encoding the 41 and 45 kilodalton (kD) isoforms of the enzyme, to create single amino acid changes in the putative ATP-binding site of Rubisco activase (Lys-107, Gln-109, and Ser-112) and in an unrelated cysteine residue (Cys-2...

2017
Javaid Y. Bhat Gabriel Thieulin-Pardo F. Ulrich Hartl Manajit Hayer-Hartl

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), the key enzyme of the Calvin-Benson-Bassham cycle of photosynthesis, requires conformational repair by Rubisco activase for efficient function. Rubisco mediates the fixation of atmospheric CO2 by catalyzing the carboxylation of the five-carbon sugar ribulose-1,5-bisphosphate (RuBP). It is a remarkably inefficient enzyme, and efforts to ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2016
Nitin Loganathan Yi-Chin Candace Tsai Oliver Mueller-Cajar

The photosynthetic CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) is inhibited by nonproductive binding of its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates. Reactivation requires ATP-hydrolysis-powered remodeling of the inhibited complexes by diverse molecular chaperones known as rubisco activases (Rcas). Eukaryotic phytoplankton of the red ...

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