Fragment complementation for the co-refolding of Thermotoga maritima β-glucosidase by gene splitting at non-homologous region

Kim, Bong-Jo; Mangala, Selanere L.; Muralidhara, B. K.; Hayashi, Kiyoshi

doi:10.1016/j.enzmictec.2006.06.005

Enzyme and Microbial Technology

2007

DOI: 10.1016/j.enzmictec.2006.06.005

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Fragment complementation for the co-refolding of Thermotoga maritima β-glucosidase by gene splitting at non-homologous region

Bong-Jo Kim

Selanere L. Mangala

B. K. Muralidhara

et al.

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Cited by 2 publications

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“…This phenomenon was used in studies of protein folding and in analyzing the essential recognition elements for stable folding. Folding complementation of protein fragments produced by limited proteolytic cleavage or genetic methods has been studied under both in vivo and in vitro conditions − . In 1959, Richards and Vithayathil reported that the mixture of two enzymically inactive components of modified ribonuclease can recover almost the full enzymic activity .…”

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confidence: 99%

The Native-like Interactions between SNase121 and SNase(111−143) Fragments Induce the Recovery of Their Native-like Structures and the Ability to Degrade DNA

et al. 2009

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The interactions necessary for stabilizing the folding of the N-terminal large beta-subdomain and the C-terminal small alpha-subdomain of staphylococcal nuclease (SNase) were investigated by an approach of fragment complementation. Two SNase fragments, namely, SNase121 and SNase(111-143) containing 1-121 and 111-143 residues, respectively, of native SNase, were used in this study since the sequences of the two fragments correspond to that of the beta- and alpha-subdomains of SNase. SNase121 is a largely unfolded fragment whereas SNase(111-143) is a structureless fragment. The recognition process and efficiency of complementation of SNase121 and SNase(111-143) fragments were studied by NMR and various biochemical and biophysical methods. SNase121 and SNase(111-143) can recognize each other and recover their native conformations on binding, restoring the active site and the ability to degrade DNA. The SNase121:SNase(111-143) complex showed a nuclease activity up to 30% that of native SNase. The final rigid structures of SNase121 and SNase(111-143) fragments having the folded native-like beta-subdomain and alpha-subdomain structures of SNase, respectively, in the complex form simultaneously with the complex stabilization. Studies with the mutant SNase121 and SNase(111-143) fragments reveal that the sequence elements which are essential for recognition and efficient complementation of the two fragments are also necessary for recovering the native-like interactions at the binding interface between them. The interfragment interactions that induce the structural complementation of SNase121 and SNase(111-143) likely reflect the tertiary interactions necessary to stabilize the folding of both beta- and alpha-subdomains in the native SNase.

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confidence: 99%

The Native-like Interactions between SNase121 and SNase(111−143) Fragments Induce the Recovery of Their Native-like Structures and the Ability to Degrade DNA

et al. 2009

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[Review: Prize-awarded article] Research on the Development of Innovative Application and Modifying Technology for the Carbohydrate Relating Enzymes

Hayashi

2012

Bull Appl Glycosci

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Fragment complementation for the co-refolding of Thermotoga maritima β-glucosidase by gene splitting at non-homologous region

Cited by 2 publications

References 20 publications

The Native-like Interactions between SNase121 and SNase(111−143) Fragments Induce the Recovery of Their Native-like Structures and the Ability to Degrade DNA

The Native-like Interactions between SNase121 and SNase(111−143) Fragments Induce the Recovery of Their Native-like Structures and the Ability to Degrade DNA

[Review: Prize-awarded article] Research on the Development of Innovative Application and Modifying Technology for the Carbohydrate Relating Enzymes

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