Occurrence of more than one important source of ADPglucose linked to glycogen biosynthesis in Escherichia coli and Salmonella.
To explore the possible occurrence of sources, other than GlgC, of ADPglucose linked to bacterial glycogen biosynthesis we characterized Escherichia coli and Salmonella DeltaglgCAP deletion mutants lacking the whole glycogen biosynthetic machinery. These mutants displayed the expected glycogen-less phenotype but accumulated ADPglucose. Importantly, DeltaglgCAP cells expressing the glycogen synthase encoding glgA gene accumulated glycogen. Protein chromatographic separation of crude extracts of DeltaglgCAP mutants and subsequent activity measurement analyses revealed that these cells possess various proteins catalyzing the conversion of glucose-1-phosphate into ADPglucose. Collectively these findings show that enterobacteria possess more than one important source of ADPglucose linked to glycogen biosynthesis.
Morán-Zorzano
María T
MT
Instituto de Agrobiotecnología, (CSIC, UPNA, Gobierno de Navarra), Mutiloako etorbidea zenbaki gabe, 31192 Mutiloabeti, Nafarroa, Spain.
Alonso-Casajús
Nora
N
Muñoz
Francisco J
FJ
Viale
Alejandro M
AM
Baroja-Fernández
Edurne
E
Eydallin
Gustavo
G
Pozueta-Romero
Javier
J
D000245:Adenosine Diphosphate Glucose / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D051599:Glucose-1-Phosphate Adenylyltransferase / Q000235:genetics / Q000378:metabolism; D006003:Glycogen / Q000378:metabolism* / Q000648:ultrastructure; D046529:Microscopy, Electron, Transmission; D009154:Mutation; D012475:Salmonella / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure
D000245:Adenosine Diphosphate Glucose; D006003:Glycogen; D051599:Glucose-1-Phosphate Adenylyltransferase