The Lack of Concordance in Evolutionary Pattern of Carboxysome Proteins –
Repercussions of HGT or Diverse Evolutionary Potential?
Gurpreet Kaur Sidhu1, Panchsheela Nogia1, Vandana Tomar1, Rajesh Mehrotra2 and Sandhya Mehrotra2
1Plant Molecular Biology and Biochemistry Laboratory, Birla Institute of
Technology and Science, Department of Biological Sciences, Pilani, India
2Department of Biological Sciences, Birla Institute of Technology and Science, KK Birla Goa Campus, Zuarinagar, Goa, India
*Corresponding Author: Sandhya Mehrotra, Department of Biological Sciences, Birla Institute of Technology and Science, KK Birla Goa Campus, Zuarinagar, Goa, India.
Received:
August 10, 2023; Published: September 23, 2023
Abstract
Carboxysomes are microcompartments enclosing the primary photosynthetic enzyme Ribulose 1, 5 Bisphosphate Carboxylase/Oxygenase (RuBisCO), an adaptation to help overcome the loose specificity of the latter for carbon dioxide. These carboxysomes, which exist in cyanobacteria and a few other eubacteria are composed of a protein shell wherein a well organized multi-protein assembly acts as the carbon concentrating mechanism (CCM). The present study was conducted to find out the presence/absence of the carboxysome forming proteins across various phyla of eubacteria in order to trace their evolutionary path. The analysis was conducted using the CCM proteins of Gloeobacter violaceus PCC 7421, an early diverging cyanobacterium.
While α carboxysome proteins are also found in other phyla of eubacteria such as proteobacteria, complete set of β carboxysome constituting proteins are found only in β cyanobacteria. The study supports the fact that shell proteins of carboxysomes are evolutionarily linked to shell proteins of microcompartments involved in ethanolamine utilization and propanediol utilization pathways. Moreover, the CcmM and CcmN proteins have possibly originated by domain shuffling or gene fusion like mechanisms. The CcmM, CcmN and CcmO, the multidomain proteins were found to have an evolutionary pattern different from that of CcmK and CcmL leading to cumulative effect on phylogeny of complete operon which was found to be only moderately similar to most conserved regions of genome. The latter (CcmK and CcmL) also being more conserved suggest less robustness to mistranslation possibly due to tight selection of the protein structure evidently responsible for creating an environment suitable for microcompartment pathway it encloses.
Keywords: Carbon Concentrating Mechanism; Carboxysome; BMC Domain; Domain Shuffling; Microcompartment; Evolution
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