An Escherichia coli mutant producing a truncated inactive form of GlgC synthesizes glycogen: further evidences for the occurrence of various important sources of ADPglucose in enterobacteria.

EYDALLIN, G.; MORÁN ZORZANO, MAITENA; MUÑOZ, F.; BAROJA FERNANDEZ, EDURNE; MONTERO, M.; ALONSO-CASAJÚS, N.; VIALE, ALEJANDRO MIGUEL; POZUETA ROMERO, JAVIER

Febs Letters

Elsevier

Año: 2007 vol. 581 p. 4417 - 4422

0014-5793

AC70R1-504 Escherichia coli mutants possess a glgC* gene with a nucleotide change resulting in a premature stop codon that renders a truncated, inactive form of GlgC. Cells over-expressing the wild type glgC, but not those over-expressing the AC70R1-504 glgC*, accumulated high ADPglucose and glycogen levels. AC70R1-504 mutants accumulated glycogen, whereas DeltaglgCAP deletion mutants lacking the whole glycogen biosynthetic machinery displayed a glycogen-less phenotype. AC70R1-504 cells with enhanced glycogen synthase activity accumulated high glycogen levels. By contrast, AC70R1-504 cells with high ADPG hydrolase activity accumulated low glycogen. These data further confirm that enterobacteria possess various sources of ADPglucose linked to glycogen biosynthesis.