Folia Microbiologica

, Volume 51, Issue 6, pp 547–554

Comparative studies of differential expression of chitinolytic enzymes encoded bychiA, chiB, chiC andnagA genes inAspergillus nidulans

Authors

  • T. Pusztahelyi
    • Department of Microbial Biotechnology and Cell BiologyUniversity of Debrecen
  • Z. Molnár
    • Department of Microbial Biotechnology and Cell BiologyUniversity of Debrecen
  • T. Emri
    • Department of Microbial Biotechnology and Cell BiologyUniversity of Debrecen
  • É. Klement
    • Protecomics Research GroupBiological Research Center
  • M. Miskei
    • Department of Microbial Biotechnology and Cell BiologyUniversity of Debrecen
  • J. Kerékgyártó
    • Department of Biochemistry, Faculty of ScienceUniversity of Debrecen
  • J. Balla
    • Department of Nephrology, Faculty of MedicineUniversity of Debrecen
    • Department of Microbial Biotechnology and Cell BiologyUniversity of Debrecen
Article

DOI: 10.1007/BF02931619

Cite this article as:
Pusztahelyi, T., Molnár, Z., Emri, T. et al. Folia Microbiol (2006) 51: 547. doi:10.1007/BF02931619

Abstract

N-Acetyl-d-glucosamine, chito-oligomers and carbon starvation regulatedchiA, chiB, andnagA gene expressions inAspergillus nidulans cultures. The gene expression patterns of the main extracellular endochitinase ChiB and theN-acetyl-β-d-glucosaminidase NagA were similar, and the ChiB-NagA enzyme system may play a morphological and/or nutritional role during autolysis. Alterations in the levels of reactive oxygen species or in the glutathione-glutathione disulfide redox balance, characteristic physiological changes developing in ageing and autolyzing fungal cultures, did not affect the regulation of either the growth-relatedchiA or the autolysis-coupledchiB genes although both of them were down-regulated under diamide stress. The transcription of thechiC gene with unknown physiological function was repressed by increased intracellular superoxide concentration.

Abbreviations

CBD

chitin-binding domain

CV

coefficient of variance

DCM

dry cell mass

GlcNAc

N-acetyl-d-glucosamine

(GlcNAc)2

N,N′-diacetylchitobiose

(GlcNAc)3

N,N′,N″-triacetylchitotriose

GlcNAcase

β-N-acetylhexosaminidase (N-acetyl-β-d-glucosaminidase; EC 3.2.1.52)

GSH

glutathione

GSSG

glutathione disulfide

MSB

2-methyl-1,4-naphthoquinone sodium hydrogen sulfite (‘menadione sodium bisulfite’)

NCBI

National Center for Biotechnology Information

4NPGlcNAc

4-nitrophenylN-acetyl-β-d-glucosaminide

4NP(GlcNAc)2

4-nitrophenylN,N′-diacetyl-β-d-chitobioside

4NP(GlcNAc)3

4-nitrophenylN,N′,N″-triacetyl-β-d-chitotrioside

ORF

open reading frame

PMF

peptide mass fingerprint

PSD

post-source decay

ROS

reactive oxygen species

RT-PCR

real-time polymerase chain reaction

SD

standard deviation

SDS

sodium dodecyl sulfate

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Copyright information

© Institute of Microbiology, Academy of Sciences of the Czech Republic 2006