. 2009 Dec;21(12):4044–4058. doi: 10.1105/tpc.109.069211

Table 2.

Identification of Salt-Responsive Tonoplast Proteins in M. crystallinum

Spot No.	DIGE Ave. Ratio^a	DIGE t Test^b	Gene Name Description	Accession^c	No. of Identified Peptides^d	Sequence of Identified Peptides^e	z^f	Xcorr^g	ΔCn^h	Molecular Function
131	1.80	0.011	PGH1- Enolase	Q43130/S79242	3	K.VNQIGSVTESIEAVK.M K.NVNEIIGPALVGK.D R.AAVPSGASTGVYEALELR.D	2	3.94	0.66	Glycolysis, vacuolar fusion, and trafficking
							2	3.36	0.66
							2	4.41	0.81
132	2.19	0.0046	PGH1- Enolase	Q43130/S79242	2	K.VQIVGDDLLVTNPK.R K.VNQIGSVTESIEAVK.M	2	3.99	0.77	Glycolysis, vacuolar fusion, and trafficking
						K.VQIVGDDLLVTNPK.R K.VNQIGSVTESIEAVK.M	2	2.98	0.71	Glycolysis, vacuolar fusion, and trafficking
225	1.93	0.026	VHA-d - V-ATPase subunit d	Q8GUB0/AJ439342	2	R.DVQELLEK.C K.AYLEDFYR.F	2	2.77	0.38	Primary proton pump
			VHA-d - V-ATPase subunit d			R.DVQELLEK.C K.AYLEDFYR.F	1	2.04	0.30	Primary proton pump
241	1.92	0.0084	ALF1 - Fructose bisphosphate aldolase	O04975/AF003124	5	K.TAAGKPFVEVLK.E R.FAGINVENVESNR.R K.VAPEVIAEYTVR.A K.GVVELAGTNGETTT QGLDGLGAR.C K.YADELIANAAYIGTPGK.G	2	3.53	0.60	Glycolysis
				O04975/AF003124			2	3.52	0.66
							2	3.34	0.71
							2	3.89	0.68
							2	4.63	0.71
318	3.02	0.0010	VHA-B - V-ATPase subunit B	Q8GUB5/AJ438590	2	R.QIYPPINVLPSLSR.L R.VTLFLNLANDPTIER.I	2	2.87	0.64	Primary proton pump
			VHA-B - V-ATPase subunit B	Q8GUB5/AJ438590		R.QIYPPINVLPSLSR.L R.VTLFLNLANDPTIER.I	2	3.71	0.67	Primary proton pump
414	3.32	0.0099	VHA-B - V-ATPase subunit B	Q8GUB5/AJ438590	3	K.AVVQVFEGTSGIDNK.Y K.TPVSLDMLGR.I R.TYPEEMIQTGISTIDVM NSIAR.G	2	5.38	0.70	Primary proton pump
							2	2.85	0.70
							3	5.10	0.51

Protein spots chosen for MS/MS analysis met the following criteria: >1.5-fold change (P ≤ 0.05); n = 3; t test (P ≤ 0.03).

Average ratios of abundance of salt-treated tonoplast relative to the untreated control represent data from three separate experiments.

Student's t test P values are given as a measure of confidence for the ratio of each spot measured.

UniProtKB/GenBank accession numbers.

Number of matched peptides from MS/MS. Proteins were identified by two or more unique peptides.

The amino acid residues appearing before and after the periods correspond to the residues proceeding and following the peptide in the protein sequence, and the asterisks within the peptide sequence indicate a differential modification on the preceding amino acid.

The charge state of the candidate peptide.

For data validation, we accepted spectra with SEQUEST cross-correlation scores (Xcorr) of at least 2.5 for doubly and 3.5 for triply charged ions.

SEQUEST ΔCn value gives the difference of the cross-correlation scores between the best hit and the following hits.