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Tissue‐specific glycogen branching isoenzymes in a multicellular prokaryote, Streptomyces coelicolor A3(2)
Author(s) -
Bruton Celia J.,
Plaskitt Kitty A.,
Chater Keith F.
Publication year - 1995
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1995.mmi_18010089.x
Subject(s) - streptomyces coelicolor , biology , glycogen , glycogen branching enzyme , biochemistry , prokaryote , hypha , streptomyces , multicellular organism , mycelium , isozyme , bacteria , enzyme , glycogen phosphorylase , microbiology and biotechnology , gene , genetics , botany
In the overtly differentiated colonies of Streptomyces coelicolor A3(2), discrete phases of glycogen synthesis are found at the vegetative/aerial mycelium boundary (phase I) and in the immature spore chains at aerial hyphal tips (phase II). We have characterized two S. coelicolor glgB genes encoding glycogen branching enzyme, which are well separated in the genome. Disruption of glgB I led to the formation of abnormal polyglucan deposits at phase I, with phase II remaining normal, whereas disruption of glgB II interfered specifically with phase II deposits, and not with those of phase I. Thus, each branching enzyme isoform is involved in a different phase of glycogen synthesis. This situation contrasts with that in simple bacteria, which typically have a single set of enzymes for glycogen metabolism, and more closely resembles that in plants.