title: Acidic proteome of growing and resting Lactococcus lactis metabolizing maltose.
abstract: The acidic proteome of Lactococcus lactis grown anaerobically was compared for three different growth conditions: cells growing on maltose, resting cells metabolizing maltose, and cells growing on glucose. In maltose metabolizing cells several proteins were up-regulated compared with glucose metabolizing cells, however only some of the up-regulated proteins had apparent relation to maltose metabolism. Cells growing on maltose produced formate, acetate and ethanol in addition to lactate, whereas resting cells metabolizing maltose and cells growing on glucose produced only lactate. Increased levels of alcohol-acetaldehyde dehydrogenase (ADH) and phosphate acetyltransferase (PTA) in maltose-growing cells compared with glucose-growing cells coincided with formation of mixed acids in maltose-growing cells. The resting cells did not grow due to lack of an amino acid source and fermented maltose with lactate as the sole product, although ADH and PTA were present at high levels. The maltose consumption rate was approximately three times lower in resting cells than in exponentially growing cells. However, the enzyme levels in resting and growing cells metabolizing maltose were similar, which indicates that the difference in product formation in this case is due to regulation at the enzyme level. The levels of 30S ribosomal proteins S1 and S2 increased with increasing growth rate for resting cells metabolizing maltose, maltose-growing cells and glucose-growing cells. A modified form of HPr was synthesized under amino acid starvation. This is suggested to be due to alanine misincorporation for valine, which L. lactis is auxotrophic for. L. lactis conserves the protein profile to a high extent, even after prolonged amino acid starvation, so that the protein expression profile of the bacterium remains almost invariant.
authors.affiliation: Applied Microbiology, Lund University, Sweden.
authors.forename: Johan
authors.initials: J
authors.lastname: Palmfeldt
authors.forename: Fredrik
authors.initials: F
authors.lastname: Levander
authors.forename: Bärbel
authors.initials: B
authors.lastname: Hahn-Hägerdal
authors.forename: Peter
authors.initials: P
authors.lastname: James
mesh_terms: D000085:Acetates / Q000737:chemistry; D000438:Alcohols / Q000737:chemistry; D000445:Aldehyde Oxidoreductases / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D003600:Cytosol / Q000737:chemistry; D015180:Electrophoresis, Gel, Two-Dimensional; D000431:Ethanol / Q000737:chemistry; D005285:Fermentation; D005947:Glucose / Q000737:chemistry; D006019:Glycolysis; D007091:Image Processing, Computer-Assisted; D019344:Lactic Acid / Q000737:chemistry; D013294:Lactococcus lactis / Q000201:enzymology / Q000378:metabolism*; D008320:Maltose / Q000737:chemistry*; D008956:Models, Chemical; D010709:Phosphate Acetyltransferase / Q000737:chemistry; D010733:Phosphoglucomutase / Q000737:chemistry; D021381:Protein Transport; D020543:Proteome; D040901:Proteomics / Q000379:methods*; D011773:Pyruvates / Q000737:chemistry; D012269:Ribosomal Proteins / Q000737:chemistry; D013696:Temperature; D015854:Up-Regulation
chemical_list: D000085:Acetates; D000438:Alcohols; D020543:Proteome; D011773:Pyruvates; D012269:Ribosomal Proteins; D019344:Lactic Acid; D000431:Ethanol; D008320:Maltose; D000445:Aldehyde Oxidoreductases; C018699:aldehyde dehydrogenase (NAD(P)+); D010709:Phosphate Acetyltransferase; D010733:Phosphoglucomutase; D005947:Glucose