Table 1.

Lysine-acetylated β and β' peptides

Lysine-acetylated β peptides identified from glucose-exposed wild-type cells
Sequence	Prob	SEQUEST XCorr	SEQUEST ΔCn	Observed Precursor m/z	Actual Peptide Mass (MW)	Charge	Delta PPM
(R)DNK₂₃₆(+42)LQmELVPER(L)	95%	2.955	0.481	510.5923	1528.76	3	−0.4136
(R)QLEK₂₇₉(+42)DDVK(L)^*	95%	2.407	0.4241	508.7665	1015.52	2	−0.3027
(K)VTPK₈₉₀(+42)GETQLTPEEK(L)	95%	3.296	0.6551	799.9181	1597.82	2	0.8714
(R)AIFGEK₉₀₉(+42)ASDVK(D)^*	95%	3.424	0.6959	603.8215	1205.63	2	−0.7829
(K)ASDVK₉₁₄(+42)DSSLR(V)^*	95%	3.105	0.3712	560.2856	1118.56	2	−0.08906
(R)ALEIEEmQLK₉₅₄(+42)QAK(K)	95%	3.883	0.6378	786.9191	1571.82	2	0.2837
(R)AVLVAGGVEAEK₉₈₈(+42)LDK(L)	95%	4.315	0.7414	770.9325	1539.85	2	−0.3886
(K)LDK₉₉₁(+42)LPR(D)^*	95%	1.741	0.3937	392.2397	782.4648	2	−0.5344
(R)K₁₀₃₅(+42)ITQGDDLAPGVLK(I)	95%	3.136	0.5483	748.9197	1495.82	2	−0.07396
(R)mNIGQILETHLGmAAK₁₁₂₂(G)	95%	3.105	0.4271	600.9708	1799.89	3	−0.3436
(K)INAmLK₁₁₃₃(+42)QQQEVAK(L)	95%	4.660	0.6422	779.9177	1557.82	2	1.362
(K)QQQEVAK₁₁₄₀(+42)LR(E)^*	95%	2.559	0.5444	571.3196	1140.62	2	−0.4438
(R)K₁₁₇₈(+42)GmPIATPVFDGAK(E)	95%	3.851	0.6688	745.3899	1488.77	2	0.1888
(K)ELLK₁₂₀₀(+42)LGDLPTSGQIR(L)	95%	4.029	0.5342	841.4792	1680.94	2	1.418
(R)STGSYSLVTQQPLGGK₁₂₆₂(+42) AQFGGQR(F)	95%	4.335	0.5947	803.744	2408.21	3	0.543

Lysine-acetylated β’ peptides identified from glucose-exposed wild-type cells

Sequence	Prob	SEQUEST XCorr	SEQUEST ΔCn	Observed Precursor m/z	Actual Peptide Mass (MW)	Charge	Delta PPM

(K)AQTK₁₃(+42)TEEFDAIK(I)^*	95%	3.134	0.5511	711.8596	1421.70	2	0.4564
(K)K₄₀(+42)PETINYR(T)	95%	1.857	0.3906	531.7829	1061.55	2	0.5715
(R)GLATTIK₃₉₅(+42)AAK(K)	95%	2.728	0.654	508.3111	1014.61	2	0.1017
(K)GEGmVLTGPK₅₃₁(+42)EAER(L)	95%	3.620	0.5413	766.3754	1530.74	2	0.8169
(K)TSLK₅₇₀(+42)DTTVGR(A)	95%	2.799	0.4491	560.3032	1118.59	2	−1.289
(R)SGASVGIDDmVIPEK₆₄₉(+42)K(H)	95%	3.297	0.5722	852.4306	1702.85	2	0.9404
(R)AAAESSIQVK₉₅₃(+42)NK(G)	95%	3.437	0.5779	644.3492	1286.68	2	0.6021
(K)GSIK₉₅₉(+42)LSNVK(S)	95%	2.737	0.5114	494.2947	986.5748	2	−1.35
(K)LSNVK₉₆₄(+42)SVVNSSGK(L)	95%	3.015	0.6372	680.8746	1359.73	2	−0.8405
(R)NTELK₉₈₃(+42)LIDEFGR(T)	95%	3.479	0.5128	492.9273	1475.76	3	−1.452
(R)LQGVK₁₂₄₇(+42)INDK(H)	95%	1.808	0.2969	528.8063	1055.60	2	0.2463

Immunoprecipitated β and β’ proteins were separated by SDS-PAGE and β and β’ bands were digested with trypsin, as described (Chi et al., 2010). The resulting peptides were analyzed in a LTQ OrbitrapXL™ mass spectrometer, as described in the Methods section and analyzed using the Scaffold software. The table shows the Xcorr, ΔCn scores, charges, both the observed precursor m/z and actual peptide mass, and the mass deviation (delta ppm) of all 15 K-acetylated peptides detected for β and 11 K-acetylated peptides detected for β’ in the glucose-exposed samples. In these tables, the CID MS/MS spectra of the acetylated β and β’ peptides are shown in Tables S1 and S2, respectively. The complete b and y ion series are cognizable and labelled in red and blue, respectively. Acetylated peptides detected in at least two biological replicates are underlined.

An asterisk indicates acetylated peptides identified in samples collected from glucose-exposed yfiQ mutants (Supplemental Tables S6 and S7). None of these peptides was detected in the absence of glucose (Supplemental Tables S4, S5, S9 and S10).