Proteome analysis of Aspergillus niger: Lactate added in starch-containing medium can increase production of the mycotoxin fumonisin B2by modifying acetyl-CoA metabolism

Sørensen, Louise M; Lametsch, Rene; Andersen, Mikael R; Nielsen, Per V; Frisvad, Jens C

doi:10.1186/1471-2180-9-255

Table 3 Identified proteins with higher levels on medium with starch + lactate

From: Proteome analysis of Aspergillus niger: Lactate added in starch-containing medium can increase production of the mycotoxin fumonisin B₂by modifying acetyl-CoA metabolism

Protein	Spot		Identification¹							Expression
Annotation²	Id.	Mass kDa³	Database	Acc. no.	Mass kDa	pI	MP	Score	SC %	Cl. no.	Profile
Alpha-amylase, extracellular	6601	53	NCBInr	A2QL05	55⁶	4.5	5	315	13	35
Fatty acid synthase subunit alpha	6465	76⁴	NCBInr	A2Q7B6	205	5.9	10	387	5	35
Glucose-6-phosphate 1-dehydrogenase	6561	59	Swiss-Prot	P48826	59	6.2	3	130	7	35
Glutamine synthetase	6714	42	NCBInr	A2Q9R3	42	5.5	4	290	16	4
Heat shock protein Hsp70	6481	73	NCBInr	A2QPM8	70	5.1	5	198	12	4
Isocitrate dehydrogenase [NADP], mitochondrial, precursor	6644	48	Swiss-Prot	P79089	56	8.5	8	339	14	19
NADP-dependent glutamate dehydrogenase	6647	48	NCBInr	A2QHT6	50	5.8	6	382	18	4
Predicted 2-nitropropane dioxygenase	6737	41	NCBInr	A2QKX9	38⁶	5.7	4	112	17	35
Predicted glucose-methanol-choline (Gmc) oxidoreductase	6515	65	NCBInr	A2R501	65	5.4	6	373	18	35
Predicted methyltransferase	6810	36	NCBInr	A2QNF3	37	5.9	5	200	21	30
Predicted NADH cytochrome b5 reductase	6693	44	NCBInr	A2R2Z2	46	5.4	6	530	20	4
Predicted ubiquitin conjugating enzyme	7044	17	NCBInr	A2QDZ9	17	5.5	2	105	18	4
Putative 6-phosphogluconate dehydrogenase, decarboxylating	6660	47	NCBInr	Q874Q3	55	5.9	9	527	27	35
Putative aconitate hydratase, mitochondrial	6472	75	NCBInr	A2QSF4	84	6.2	7	278	11	35
Putative heat shock protein Ssc1, mitochondrial	6487	71	NCBInr	A2R7X5	72	5.6	5	282	9	4
Putative histidine biosynthesis trifunctional protein	6413	101⁵	NCBInr	A2QAS4	92	5.4	2	147	3	4
Putative inositol-1-phosphate synthase	6573	57	NCBInr	A2QV05	58	5.7	2	62	4	35
Putative ketol-acid reductoisomerase, mitochondrial	6730	41	NCBInr	A2QU08	45⁶	8.9	8	467	17	35
Putative oxoglutarate dehydrogenase	6408	101⁵	NCBInr	A2QIU5	119	6.3	10	349	8	35
Putative peroxiredoxin pmp20, peroxisomal membrane	7000	22	NCBInr	A2R0G9	19	5.4	8	610	54	4
Putative peroxiredoxin Prx1, mitochondrial	6944	28	NCBInr	A2QIF8	23	5.2	5	224	22	4
Putative pyruvate dehydrogenase E1 component subunit alpha, mitochondrial precurser	7028	18⁴	NCBInr	A2QPI1	45	7.6	2	160	7	30
Putative transaldolase	6787	38	NCBInr	A2QMZ4	36	5.6	5	319	20	4
Putative transketolase	6471	75	NCBInr	Q874Q5	75	6.0	6	246	11	4
Thioredoxin reductase	6680	45	NCBInr	A2Q9P0	39	5.2	6	449	22	4
Uncharacterised protein	6965	26	NCBInr	A2QDU1	19	5.4	3	147	15	4
Uncharacterised protein	6591	55	NCBInr	A2QDX8	57	5.8	10	601	23	4
Uncharacterised protein	6592	55	NCBInr	A2QDX8	57	5.8	10	717	25	4
Uncharacterised protein	7059	16	NCBInr	A5ABN7	26	10.3	2	145	14	35
Uncharacterised protein	7092	13⁵	NCBInr	A2QSA8	13	5.2	2	249	35	4

List of identified proteins showing from left to right: Protein name, spot id and observed mass on gels, database, UniProt KB accession number, expected mass and isoelectric point (pI), number of matching peptide sequences (MP), Mowse Score (Score) and sequence coverage (SC), cluster and graph showing protein levels (average relative spot volume ± standard deviation) on media containing 3% starch (left/blue), 3% starch + 3% lactate (middle/purple) and 3% lactate (right/red).
1) Identification was based on Mascot MS/MS Ion Search using sequence data from the databases Swiss-Prot or NCBInr. Protein matches with significant (p < 0.05) Mowse Scores and ≥ 2 matching peptides were regarded as possible candidates for identification.
2) Annotation of uncharacterised proteins was based on sequence homology to characterised Swiss-Prot proteins using BlastP. Proteins were given a full annotation if they had > 80% sequence identity to a characterised Swiss-Prot protein or a putative annotation if they had 50-80% sequence identity to a characterised protein. Remaining proteins were assigned a "predicted" function if InterPro domains were predicted using InterProScan.
3) Observed mass on reference gel calibrated with molecular weight standards (14.4-97.4 kDa).
4) The spot is most likely a fragment as the retrieved peptides were localized in one of the ends of the protein sequence.
5) Mass above or below calibration range
6) The protein is predicted to contain a signal peptide.
7) The protein is predicted to be glycosylated.

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