Analysis of 39 cyanobacterial species reveals rbcx subunit to be present between L and S Subunits

JOURNAL OF ADVANCES IN BIOLOGY

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Field Value
 
Title Analysis of 39 cyanobacterial species reveals rbcx subunit to be present between L and S Subunits
 
Creator Mehrotra, Rajesh
Siddhu, Gurpreet Kaur
Rashmi, Mis.
Mehrotra, Rajesh
Mehrotra, Sandhya
 
Description The impact of greater oxidation event on RuBisCo has been tremendous. It has led to the competition between carbon dioxide and oxygen at the active site the enzyme. Cyanobacteria developed strategies to combat this change by concentrating carbon dioxide in organelles called carboxysomes. RbCx helps in proper folding of RuBisCO by interacting with Rbcl. However, it is not an absolute requirement for RuBbisCO to attain proper folding only with the aid of RbCx. RbCx has a chaperone like activity. The present analysis led to the finding that in case of cyanobacterial species lacking RbCx contains multitude of protein showing homology to chaperone like proteins. These proteins might be playing the same role as RbCx in these cyanobacterial species to help RuBisCo acquiring proper folding. Analyses also indicated that in general the rbcx motif to be present between rbcl and rbcs.
 
Publisher CIRWORLD
 
Date 2016-12-28
 
Type info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Peer-reviewed Article
 
Format application/pdf
 
Identifier http://cirworld.com/index.php/jab/article/view/4585
 
Source JOURNAL OF ADVANCES IN BIOLOGY; Vol 7 No 3; 1420-1426
2347-6893
 
Language eng
 
Relation http://cirworld.com/index.php/jab/article/view/4585/4467
 
Rights Copyright (c) 2016 JOURNAL OF ADVANCES IN BIOLOGY
http://creativecommons.org/licenses/by/4.0
 

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