TITLE:
Differential Regulation of Proteins and a Possible Role for Manganese Superoxide Dismutase in Bioluminescence of Panellus stipticus Revealed by Suppression Subtractive Hybridization
AUTHORS:
Galina A. Vydryakova, John Bissett
KEYWORDS:
Panellus stipticus, Mushroom Bioluminescence, Suppression Subtractive Hybridization, Manganese Superoxide Dismutase
JOURNAL NAME:
Advances in Microbiology,
Vol.6 No.9,
August
2,
2016
ABSTRACT: Suppression
subtractive hybridization (SSH) was employed to investigate bioluminescence in Panellus stipticus (Bull.) P. Karst. by
detecting proteins differentially expressed in bioluminescent and luminescent
strains. Comparisons of luminescent and non-luminescent monokaryon cultures of
North American strains revealed differences in transcript levels of proteins
responsible for post-translational modification (PTM) of enzymes. A similar
comparison of a luminescent strain of P.
stipticus from North America with a non-luminescent European strain
revealed the presence of extracellular manganese superoxide dismutase (MnSOD)
in the luminescent form, in addition to proteins involved in PTM. The
application of MnSOD-specific inhibitors to luminescent mycelium resulted in
the rapid loss of luminescence. The relevance to luminescence of proteins
involved in PTM is discussed, together with a possible role for MnSOD that
considers the potential for SODs to form stable complexes with catechols
revealed in previously published research. In light of the recent discovery
that hispidine may be the precursor of fungal luciferin, we consider a hypothetical
mechanism for fungal luminescence in which the ο-hydroquinone moiety of a
hispidine derivative ligates with the extracellular form of MnSOD producing a
semiquinone-radical complex, with the resultant semiquinonato complex
potentially reacting with molecular oxygen or other reactive oxygen species to
produce sufficiently excited intermediates to emit light on relaxation.