NDLI: Expression and Biological Properties of a Novel Methionine Sulfoxide Reductase A in Tobacco (Nicotiana tabacum)

Content Provider	Springer Nature Link
Author	Liu, Likun Wang, Myeong Hyeon
Copyright Year	2013
Abstract	Methionine (Met) residues in proteins/peptides are extremely susceptible to oxidation mediated by reactive oxygen species, resulting in the formation of methionine sulfoxide, which could be inversely reduced back to Met by methionine sulfoxide reductase (MSR). In the present study, an A-type MSR gene, termed NtMSRA4, was isolated from tobacco (Nicotiana tabacum). Sequence analysis of NtMSRA4 amino acid sequence indicated that the gene, encoded a polypeptide with a molecular weight of 21 kDa, possessed the highly conserved motif, ‘GCFWG’ in the N-terminus and ‘KGCNDPIRCY’ motif in the C-terminus respectively. Substrate specific analysis revealed that recombinant NtMSRA4 protein could reduce specifically S-isomer of Dabsyl-MetSO to Dabsyl-Met in vitro using dithiothreitol as an electron donor. Enzymatic properties analysis showed that the temperature of 42 °C and pH 9.0 were optimum for NtMSRA4 activity. The K $_{m}$ and K $_{cat}$ values of NtMSRA4 were determined to be 40.04 μM and 0.048 S$^{−1}$ in the thioredoxin dependent reduction system. Overexpression of NtMSRA4 in E. coli cells enhanced resistance to H$_{2}$O$_{2}$ toxicity. Subcellular localization result showed that NtMSRA4 was located in the chloroplast. The expression level of NtMSRA4 was affected differently after exposure to various abiotic stresses.
Starting Page	266
Ending Page	274
Page Count	9
File Format	PDF
ISSN	15723887
Journal	The Protein Journal
Volume Number	32
Issue Number	4
e-ISSN	15734943
Language	English
Publisher	Springer US
Publisher Date	2013-04-04
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Methionine sulfoxide reductase Nicotiana tabacum NtMSRA4 Oxidative stress Enzymatic properties Bioorganic Chemistry Biochemistry Organic Chemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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