Hostname: page-component-848d4c4894-8bljj Total loading time: 0 Render date: 2024-07-06T15:42:24.674Z Has data issue: false hasContentIssue false

Proteomic identification of a fucosyltransferase from petals of milk thistle, Silybum marianum

Published online by Cambridge University Press:  16 July 2014

Siddhartha Kumar Mishra
Affiliation:
CSIR – Central Institute of Medicinal and Aromatic Plants, PO – CIMAP, Lucknow226 015, India
Neelam S. Sangwan
Affiliation:
CSIR – Central Institute of Medicinal and Aromatic Plants, PO – CIMAP, Lucknow226 015, India
Manoj Kumar Srivastava
Affiliation:
Department of Biochemistry, J.C. Bose Institute of Life Sciences, Bundelkhand University, Jhansi284 128, India
Bhawana Mishra
Affiliation:
CSIR – Central Institute of Medicinal and Aromatic Plants, PO – CIMAP, Lucknow226 015, India
Rajender Singh Sangwan*
Affiliation:
CSIR – Central Institute of Medicinal and Aromatic Plants, PO – CIMAP, Lucknow226 015, India
*
* Corresponding author. E-mail: sangwan.lab@gmail.com

Abstract

Fucosyltransferases are a group of enzymes that catalyse the transfer of l-fucose from a donor substrate to an acceptor molecule. Silybum marianum is also called ‘milk thistle’ due to its characteristic flower shape. It produces two major flavonoids: silymarin and silybin. The plant and its major secondary metabolites are used for treatment/recovery after chronic liver disease, liver rehabilitation after hepatitis and treatment of gallbladder disease. These compounds also act as antioxidants for scavenging free radicals and inhibiting lipid peroxidation. We identified two peptide motifs (YYEAYLSHADEK and TTPDPSCGR designated as motif 1 and motif 2, respectively) of a fucosyltransferase derived from S. marianum that are highly conserved in its counterparts across the plant species and sources. The nature and properties of the motifs are discussed in terms of their putative participation in catalysis and enzyme/active site conformation.

Type
Research Article
Copyright
Copyright © NIAB 2014 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Costa, G, Decou, R and Lhernould, S (2007) The multigenic family of fucyltransferase from poplar tree. EMBL/GenBank/DDBJ databases.Google Scholar
Levy, S, York, WS, Stuike-Prill, R, Meyer, B and Staehelin, LA (1991) Simulations of the static and dynamic molecular conformations of xyloglucan. The role of the fucosylated sidechain in surface-specific sidechain folding. Plant Journal 1: 195215.Google Scholar
Levy, S, Maclachlan, G and Staehelin, LA (1997) Xyloglucan sidechains modulate binding to cellulose during in vitro binding assays as predicted by conformational dynamics simulations. Plant Journal 11: 373386.CrossRefGoogle ScholarPubMed
Lin, X, Kaul, S, Rounsley, S, Shea, TP, Benito, MI and Town, CD (1999) Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana . Nature 402: 761768.Google Scholar
Ma, B, Simala-Grant, JL and Taylor, DE (2006) Fucosylation in prokaryotes and eukaryotes. Glycobiology 16: 158R184R.Google Scholar
Matsumoto, T, Wu, J, Kanamori, H, Katayose, Y, Fujisawa, M and Namiki, N (2005) The map-based sequence of the rice genome. Nature 436: 793800.Google Scholar
Mishra, SK, Sangwan, NS and Sangwan, RS (2013a) Comparative physico-kinetic properties of a homogenous purified β-glucosidase from Withania somnifera leaf. Acta Physiologiae Plantarum 35: 14391451.Google Scholar
Mishra, SK, Sangwan, NS and Sangwan, RS (2013b) Purification and physicokinetic characterization of a gluconolactone inhibition-insensitive β-glucosidase from Andrographis paniculata nees. Leaf. Preparative Biochemistry and Biotechnology 43: 481499.CrossRefGoogle ScholarPubMed
Mishra, SK, Sangwan, NS and Sangwan, RS (2013c) Physico-kinetic and functional features of a novel β-glucosidase isolated from milk thistle (Silybum marianum Gaertn.) flower petals. Journal of Plant Biochemistry and Biotechnology: 110. Doi:10.1007/s13562-013-0221-y.Google Scholar
Perrin, RM, DeRocher, AE, Bar-Peled, M, Zeng, W, Norambuena, L, Orellana, A, Raikhel, NV and Keegstra, K (1999) Xyloglucan fucosyltransferase, an enzyme involved in plant cell wall biosynthesis. Science 284: 19761979.CrossRefGoogle ScholarPubMed
Ricketts, LM, Dlugosz, M, Luther, KB, Haltiwanger, RS and Majerus, EM (2007) O-Fucosylation is required for ADAMTS13 secretion. Journal of Biological Chemistry 282: 1701417023.Google Scholar
Sarria, R, Wagner, TA, O'Neill, M, Faik, A, Wilkerson, C, Keegstra, K and Raikhel, NV (2001) Characterization of a family of Arabidopsis genes related to xyloglucan fucosyltransferase. Plant Physiology 127: 15951606.Google Scholar
Sasaki, T, Matsumoto, T and Katayose, Y (2002) Oryza sativa nipponbare (GA3) genomic DNA, chromosome 7, PAC clone: P0446F04. EMBL/GenBank/DDBJ databases.Google Scholar