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Identification of Binding Partners of CsaA - an Archaeal Chaperonic Protein of Picrophilus Torridus

Author(s):

Neelja Singhal, Archana Sharma, Manisha Aswal, Nirpendra Singh, Manish Kumar and Manisha Goel*   Pages 1 - 5 ( 5 )

Abstract:


Background: CsaA is among the few chaperones which are present in both bacteria and archaea, but absent in eukaryotes. There are no reports on interactome analysis of CsaA from archaea, till date. Identification of binding partners of CsaA might be helpful in understanding CsaA-associated processes in Picrophilus torridus– an extreme thermoaci-dophilic euryarchaeon.

Objectives: The present study was conducted to identify the binding partners of CsaA of P. torridus (PtCsaA).

Methods: The binding partners of PtCsaA were isolated and identified using a pull down assay and liquid chromatography-mass spectrometry (LC-MS).

Results: The results revealed twelve potential binding partners of CsaA. These were thermosome subunits (Q6KZS2 and Q6L132), nascent polypeptide-associated complex protein (Q6L1N3), elongation factor 1-alpha (Q6L202), uncharacterized protein (Q6L0Y6), citrate synthase (Q6L0M8), asparaginyl-tRNA synthetase (Q6L0M5), succinyl-CoA synthetase beta chain (Q6L0B4), pyruvate ferredoxin oxidoreductase alpha and beta chain proteins (Q6KZA7 and Q6KZA6, respectively), malate dehydrogenase (Q6L0C3) and reversed fumarylacetoacetase (Q6KZ97). Functional categorization revealed that of these, six proteins were involved in energy metabolic pathways, three were archaeal chaperones, two were involved in trans-lation and one might be a transcription regulator. STRING-based analysis of the protein-protein interactions of the experi-mental interactome revealed strong interactions among them.

Conclusion: PtCsaA might be a multifaceted protein which besides translation might also play important role in metabolic processes of P. torridus. However, further experiments investigating the binding partners of CsaA in other archaea are re-quired for a better understanding of CsaA-associated processes in archaea.

Keywords:

Chaperone, protein-protein interactions, binding partners, liquid chromatography mass spectrometry

Affiliation:

Department of Biophysics, University of Delhi South Campus, New Delhi 110021;, Department of Biophysics, University of Delhi South Campus, New Delhi 110021;, Department of Biophysics, University of Delhi South Campus, New Delhi 110021;, Regional Centre for Biotechnology, NCR-Biotech Science Cluster, Faridabad,, Department of Biophysics, University of Delhi South Campus, New Delhi 110021;, Department of Biophysics, University of Delhi South Campus, New Delhi 110021;



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