Effects of heat shock protein CLPC’S ɑ4-β2 loop deletion from an alkaliphilic Bacillus lehensis G1 on its stability and activity

Siti Aishah Rashid, Farah Diba Abu Bakar, Abdul Munir Abd. Murad, Rosli Md Illias

Research output: Contribution to journalArticle

Abstract

Protein loops are frequently considered as critical determinants that influence not only the function but also the structure of a protein. Bacillus lehensis G1 ClpC (WT) has a four-residue insertion at the ɑ4-β2 loop, which is absent in Bacillus subtillis ClpC. To foster a deep understanding of the significance of additional residues in the structure and function of ClpC, a deletion mutation involving residues 76-79 (∆76-79) was constructed. Circular dichroism spectroscopy was used to evaluate the structural perturbations associated with the deletion. The results demonstrated that, the precise configuration of the ɑ4-β2 loop is important for maintaining the structure and function of WT. ∆76-79 leads to severe global destabilisation and unfolding of the secondary structure of the protein, which decreases ATPase activity. The optimum temperature for ∆76-79 is 25 °C, down from 45 °C for WT. The results suggest that the additional four residues at the ɑ4-β2 loop are critical for WT’s structure and function.

Original languageEnglish
Pages (from-to)189-196
Number of pages8
JournalJurnal Teknologi
Volume79
Issue number5
DOIs
Publication statusPublished - 1 Jul 2017

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Bacilli
Proteins
Circular dichroism spectroscopy
Hot Temperature
Temperature

Keywords

  • Alkaliphilic ClpC
  • ATPase activity
  • Deletion
  • N-terminal loop
  • Secondary structure

ASJC Scopus subject areas

  • Engineering(all)

Cite this

Effects of heat shock protein CLPC’S ɑ4-β2 loop deletion from an alkaliphilic Bacillus lehensis G1 on its stability and activity. / Rashid, Siti Aishah; Abu Bakar, Farah Diba; Abd. Murad, Abdul Munir; Illias, Rosli Md.

In: Jurnal Teknologi, Vol. 79, No. 5, 01.07.2017, p. 189-196.

Research output: Contribution to journalArticle

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