Effects of mutations at Gly114 on the stability and refolding of haloarchaeal nucleoside diphosphate kinase in low salt solution

Ishibashi, Matsujiro; Iwasa, Tatsuya; Kumeda, Kouko; Arakawa, Tsutomu; Tokunaga, Masao

doi:10.1016/j.ijbiomac.2009.02.003

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Stabilization Of Unstable G114d Mutant By His-tag Sequence2

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Cited by 4 publications

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“…7). The mobility was similar to that of G114R mutant (data not shown) [11], which was stabilized the subunit assembly [10], suggesting that HisG114D mutant is also a hexameric structure under low salt. Without His-tag, it dissociates to the monomers.…”

Section: Stabilization Of Unstable G114d Mutant By His-tag Sequencesupporting

confidence: 58%

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Interaction of hexa-His tag with acidic amino acids results in facilitated refolding of halophilic nucleoside diphosphate kinase

Ishibashi

Ida

Tatsuda

et al. 2011

International Journal of Biological Macromolecules

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Section: Stabilization Of Unstable G114d Mutant By His-tag Sequencesupporting

confidence: 58%

“…When this residue was mutated to Asp, the subunit interaction was destabilized due to charge repulsion from E155 present in neighboring subunit [10,11]. We have characterized His-tag form of G114D, i.e., HisG114D.…”

Section: Stabilization Of Unstable G114d Mutant By His-tag Sequencementioning

confidence: 99%

Interaction of hexa-His tag with acidic amino acids results in facilitated refolding of halophilic nucleoside diphosphate kinase

Ishibashi

Ida

Tatsuda

et al. 2011

International Journal of Biological Macromolecules

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Halophilic Properties and their Manipulation and Application

et al. 2012

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Increase of salt dependence of halophilic nucleoside diphosphate kinase caused by a single amino acid substitution

et al. 2013

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Nucleoside diphosphate kinase (HsNDK) from an extremely halophilic archaea, Halobacterium salinarum, is composed of a homo hexamer, assembled as a trimer of basic dimeric units. It requires >2 M NaCl for refolding, although it does not require NaCl for stability or enzymatic activity below 30 °C. A HisN111L mutant with an N-terminal extension sequence containing hexa-His tag, in which Asn111 was replaced with Leu, was designed to be less stable between basic dimeric units. This mutant can lose between 6 and 12 hydrogen bonds between basic dimeric units in the hexamer structure. The HisN111L mutant had enhanced salt requirements for enzymatic activity and refolding even though the secondary structure of the HisN111L mutant was confirmed to be similar to the control, HisNDK, in low and high salt solutions using circular dichroism. We reported previously that G114R and D148C mutants, which had enhanced interactions between basic dimeric units, showed facilitated refolding and stabilization in low salt solution. The results of this study help to elucidate the process for engineering industrial enzymes by controlling subunit-subunit interactions through mutations.

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Effects of mutations at Gly114 on the stability and refolding of haloarchaeal nucleoside diphosphate kinase in low salt solution

Cited by 4 publications

References 10 publications

Interaction of hexa-His tag with acidic amino acids results in facilitated refolding of halophilic nucleoside diphosphate kinase

Interaction of hexa-His tag with acidic amino acids results in facilitated refolding of halophilic nucleoside diphosphate kinase

Halophilic Properties and their Manipulation and Application

Increase of salt dependence of halophilic nucleoside diphosphate kinase caused by a single amino acid substitution

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