Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Microbiology 155 (2009), 424-433; DOI  10.1099/mic.0.022459-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary data
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Huang, S. T.
Right arrow Articles by Hsieh, H. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Huang, S. T.
Right arrow Articles by Hsieh, H. J.
Agricola
Right arrow Articles by Huang, S. T.
Right arrow Articles by Hsieh, H. J.
Microbiology 155 (2009), 424-433; DOI  10.1099/mic.0.022459-0
© 2009 Society for General Microbiology

Cloning and heterologous expression of a novel ligninolytic peroxidase gene from poroid brown-rot fungus Antrodia cinnamomea

S. T. Huang, S. S. Tzean, B. Y. Tsai and H. J. Hsieh

Department of Plant Pathology and Microbiology, National Taiwan University, Taipei 10617, Taiwan, ROC

Correspondence
S. S. Tzean
sst{at}ntu.edu.tw
B. Y. Tsai
bieyntm{at}ntu.edu.tw

A novel ligninolytic peroxidase gene (ACLnP) was cloned and characterized from a poroid brown-rot fungus, Antrodia cinnamomea. The genomic DNA of the fungus harboured two copies of ACLnP, with a length of 2111 bp, interlaced with 12 introns, while the full-length cDNA was 1183 bp, with a 66 bp signal peptide and an ORF of 990 bp. The three-dimensional molecular structure model was comparable to that of the versatile peroxidase of Pleurotus eryngii. ACLnP was cloned into vector pQE31, successfully expressed in Escherichia coli strain M15 under the control of the T5 promoter and produced a non-glycosylated protein of about 38 kDa, pI 5.42. The native and recombinant ACLnP was capable of oxidizing the redox mediator veratryl alcohol, and also decolorized bromophenol blue and 2,6-dimethoxyphenol dyes, implicating a functional extracellular peroxidase activity. The significance of discovering a functional ACLnP gene in A. cinnamomea in terms of wood degradation and colonization capacity in its unique niche is discussed.

Abbreviations: (r,n)ACLnP, (recombinant, native) Antrodia cinnamomea ligninolytic peroxidase; BG, β-glucosidase; EBG, exo-1,3-β-glucanase; EST, expressed sequence tag; LiP, lignin peroxidase; LnP, ligninolytic peroxidase; MnP, manganese-dependent peroxidase; VA, veratryl alcohol; VP, versatile peroxidase

*Deceased.

The GenBank/EMBL/DDBJ accession numbers for the full-length cDNA sequence of the ACLnP gene and the genomic DNA sequence, including the promoter region of the cloned ACLnP gene, are EU289404 and EU526903, respectively.

Supplementary figures and tables are available with the online version of this paper.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2009 Society for General Microbiology.