Characterization of a novel Cyclophilin-type peptidylprolyl isomerase protein from sweet potato storage roots

Jung Chun Liao, Chuan Sung Chiu, Hsien Jung Chen, Shyh Shyun Huang, Wen Chi Hou, Wang Ching Lin, Yaw Huei Lin, Guan Jhong Huang

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

An antioxidant protein of cyclophilin-type peptidylprolyl isomerase (SPPPI) from sweet potato (Ipomoea batatas (L.) Lam. 'Tainong 57') storage roots was isolated by differential display. The open reading frame of this cDNA encodes a pro-protein of 260 amino acids with a predicted molecular mass of 27,658 Da (pI 9.34). A comparison of the deduced amino acid sequence of SPPPI with precursor proteins indicates 65% identity to the Arabidopsis thaliana AraPPI sequence. Computer analysis of the deduced amino acid sequences of the conserved domain revealed that the protein belonged to the plant cyclophilin-type peptidylprolyl isomerase. Genomic Southern blot analyses using the full-length SPPPI cDNA probe revealed a multigene family in the sweet potato genome. Both the corresponding mRNA and protein level were found the highest in the storage roots, followed by that in sprout. Recombinant SPPPI overproduced in E. coli (M15) was purified by Ni2+-chelated affinity chromatography. Both the peptidylprolyl isomerase and antioxidantive activity of active recombinant SPPPI were investigated. SPPPI and CP (calf thymus cytophilin, a positive control) displayed the highest ABTS (2, 2-azino-bis-(3-ethylbenzothiazoline- 6-sulfonic acid) scavenging ability (15.36 ± 0.80 and 17.79 ± 1.72%, respectively) at 100 μg/mL. In the DPPH (1, 1-diphenyl-2- picrylhydrazyl) assay, SPPPI and CP were found to have the highest radical- scavenging activity (5.78 ± 0.62 and 4.05± 0.80%, respectively) at 100 μg/mL. The Fe2+-chelating ability of SPPPI and CP was found to be the highest (12.47± 2.37 and 14.57± 0.96%) at 100 μg/mL, respectively. It was suggested that SPPPI is an excellent candidate as a lead compound for the development of reductant agents.

Original languageEnglish
Pages (from-to)315-324
Number of pages10
JournalBotanical Studies
Volume53
Issue number3
Publication statusPublished - Jul 2012

Fingerprint

peptidylprolyl isomerase
cyclophilins
sweet potatoes
proteins
amino acid sequences
computer analysis
reducing agents
Ipomoea batatas
sulfonic acid
affinity chromatography
multigene family
Southern blotting
open reading frames
Arabidopsis thaliana
calves
iron
molecular weight
Escherichia coli
genomics
antioxidants

Keywords

  • Gene expression
  • Peptidylprolyl isomerase protein
  • Recombinant protein
  • Sweet potato

ASJC Scopus subject areas

  • Plant Science

Cite this

Liao, J. C., Chiu, C. S., Chen, H. J., Huang, S. S., Hou, W. C., Lin, W. C., ... Huang, G. J. (2012). Characterization of a novel Cyclophilin-type peptidylprolyl isomerase protein from sweet potato storage roots. Botanical Studies, 53(3), 315-324.

Characterization of a novel Cyclophilin-type peptidylprolyl isomerase protein from sweet potato storage roots. / Liao, Jung Chun; Chiu, Chuan Sung; Chen, Hsien Jung; Huang, Shyh Shyun; Hou, Wen Chi; Lin, Wang Ching; Lin, Yaw Huei; Huang, Guan Jhong.

In: Botanical Studies, Vol. 53, No. 3, 07.2012, p. 315-324.

Research output: Contribution to journalArticle

Liao, JC, Chiu, CS, Chen, HJ, Huang, SS, Hou, WC, Lin, WC, Lin, YH & Huang, GJ 2012, 'Characterization of a novel Cyclophilin-type peptidylprolyl isomerase protein from sweet potato storage roots', Botanical Studies, vol. 53, no. 3, pp. 315-324.
Liao, Jung Chun ; Chiu, Chuan Sung ; Chen, Hsien Jung ; Huang, Shyh Shyun ; Hou, Wen Chi ; Lin, Wang Ching ; Lin, Yaw Huei ; Huang, Guan Jhong. / Characterization of a novel Cyclophilin-type peptidylprolyl isomerase protein from sweet potato storage roots. In: Botanical Studies. 2012 ; Vol. 53, No. 3. pp. 315-324.
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abstract = "An antioxidant protein of cyclophilin-type peptidylprolyl isomerase (SPPPI) from sweet potato (Ipomoea batatas (L.) Lam. 'Tainong 57') storage roots was isolated by differential display. The open reading frame of this cDNA encodes a pro-protein of 260 amino acids with a predicted molecular mass of 27,658 Da (pI 9.34). A comparison of the deduced amino acid sequence of SPPPI with precursor proteins indicates 65{\%} identity to the Arabidopsis thaliana AraPPI sequence. Computer analysis of the deduced amino acid sequences of the conserved domain revealed that the protein belonged to the plant cyclophilin-type peptidylprolyl isomerase. Genomic Southern blot analyses using the full-length SPPPI cDNA probe revealed a multigene family in the sweet potato genome. Both the corresponding mRNA and protein level were found the highest in the storage roots, followed by that in sprout. Recombinant SPPPI overproduced in E. coli (M15) was purified by Ni2+-chelated affinity chromatography. Both the peptidylprolyl isomerase and antioxidantive activity of active recombinant SPPPI were investigated. SPPPI and CP (calf thymus cytophilin, a positive control) displayed the highest ABTS (2, 2-azino-bis-(3-ethylbenzothiazoline- 6-sulfonic acid) scavenging ability (15.36 ± 0.80 and 17.79 ± 1.72{\%}, respectively) at 100 μg/mL. In the DPPH (1, 1-diphenyl-2- picrylhydrazyl) assay, SPPPI and CP were found to have the highest radical- scavenging activity (5.78 ± 0.62 and 4.05± 0.80{\%}, respectively) at 100 μg/mL. The Fe2+-chelating ability of SPPPI and CP was found to be the highest (12.47± 2.37 and 14.57± 0.96{\%}) at 100 μg/mL, respectively. It was suggested that SPPPI is an excellent candidate as a lead compound for the development of reductant agents.",
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N2 - An antioxidant protein of cyclophilin-type peptidylprolyl isomerase (SPPPI) from sweet potato (Ipomoea batatas (L.) Lam. 'Tainong 57') storage roots was isolated by differential display. The open reading frame of this cDNA encodes a pro-protein of 260 amino acids with a predicted molecular mass of 27,658 Da (pI 9.34). A comparison of the deduced amino acid sequence of SPPPI with precursor proteins indicates 65% identity to the Arabidopsis thaliana AraPPI sequence. Computer analysis of the deduced amino acid sequences of the conserved domain revealed that the protein belonged to the plant cyclophilin-type peptidylprolyl isomerase. Genomic Southern blot analyses using the full-length SPPPI cDNA probe revealed a multigene family in the sweet potato genome. Both the corresponding mRNA and protein level were found the highest in the storage roots, followed by that in sprout. Recombinant SPPPI overproduced in E. coli (M15) was purified by Ni2+-chelated affinity chromatography. Both the peptidylprolyl isomerase and antioxidantive activity of active recombinant SPPPI were investigated. SPPPI and CP (calf thymus cytophilin, a positive control) displayed the highest ABTS (2, 2-azino-bis-(3-ethylbenzothiazoline- 6-sulfonic acid) scavenging ability (15.36 ± 0.80 and 17.79 ± 1.72%, respectively) at 100 μg/mL. In the DPPH (1, 1-diphenyl-2- picrylhydrazyl) assay, SPPPI and CP were found to have the highest radical- scavenging activity (5.78 ± 0.62 and 4.05± 0.80%, respectively) at 100 μg/mL. The Fe2+-chelating ability of SPPPI and CP was found to be the highest (12.47± 2.37 and 14.57± 0.96%) at 100 μg/mL, respectively. It was suggested that SPPPI is an excellent candidate as a lead compound for the development of reductant agents.

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