Regulation of cellobiase secretion in Termitomyces clypeatus by co-aggregation with sucrase.

Abstract:

:Regulated secretory proteins are sorted via selective co-aggregation in eukaryotes. Cellobiase (C) of the filamentous fungus Termitomyces clypeatus remained co-aggregated with sucrase (S), and only one isoform of each of the enzymes was present in intra- and extracellular extracts. Kinetics of secretion of sucrase increased in vivo and in vitro in secreting (Sc) medium and decreased under non-secreting (NSc) conditions similar to those observed for cellobiase. In the Sc condition, total enzyme production and activity ratios of cellobiase and sucrase (C/S) in cell-bound, extra- and intracellular preparations increased with time and were significantly higher from those obtained in non-secretory media. It was concluded that secretion of sucrase in culture medium is under same cellular regulation as that of cellobiase, and sucrase is involved in regulating extracellular release of cellobiase through co-aggregation in the fungus.

journal_name

Curr Microbiol

journal_title

Current microbiology

authors

Mukherjee S,Khowala S

doi

10.1007/s00284-001-7001-y

keywords:

subject

Has Abstract

pub_date

2002-07-01 00:00:00

pages

70-3

issue

1

eissn

0343-8651

issn

1432-0991

journal_volume

45

pub_type

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