Open AccessCytoplasmic Escherichia coli ADP sugar pyrophosphatase binds to cell membranes in response to extracellular signals as the cell population density increases
Author(s) -
MoránZorzano María Teresa,
Montero Manuel,
Muñoz Francisco José,
AlonsoCasajús Nora,
Viale Alejandro Miguel,
Eydallin Gustavo,
Sesma María Teresa,
BarojaFernández Edurne,
PozuetaRomero Javier
Publication year - 2008
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2008.01319.x
Subject(s) - biochemistry , biology , glycogen , population , rpos , escherichia coli , glycogen branching enzyme , glycogen phosphorylase , gene expression , gene , promoter , demography , sociology
ADP sugar pyrophosphatase (AspP) is a member of the ‘Nudix’ (Nucleoside diphosphate linked to some other moiety X) hydrolase family of enzymes that catalyzes the hydrolytic breakdown of ADP‐glucose (ADPG) linked to glycogen biosynthesis. In a previous work, we showed that AspP activity is strongly enhanced by both glucose‐1,6‐bisphosphate and nucleotide–sugars, and by macromolecular crowding. In this work, we show that AspP binds to cell membranes as the bacterial population density increases, c . 30% of the total enzyme remaining membrane associated as glycogen depletes during the stationary phase. This process is not dependent on the stationary transcription factor RpoS, the producer of the bacterial quorum‐sensing autoinducer 2 (LuxS), the presence of glycogen granules or glucose availability, but is stimulated by small soluble heat‐labile molecule(s) occurring in cell‐free spent supernatants of stationary cultures that are acid stabile and base labile. These data further point to AspP as a highly regulated enzyme, and provide a first set of evidences indicating that glycogen metabolism is subjected to regulation by intercellular communication in Escherichia coli .