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. Author manuscript; available in PMC: 2007 Aug 28.
Published in final edited form as: J Mol Biol. 2007 Mar 6;368(5):1332–1344. doi: 10.1016/j.jmb.2007.02.078

Table 2.

Disulfide bonded P. aerophilum proteins and complexes identified from 2D gels.

Gene Protein Spot No. Cysteines Likely Disulfides#
PAE2842 Hypothetical protein 1 3 (57, 131, 144) Potential heterocomplex
PAE3103 NusG, transcription antitermination 2 1 (6) Probable heterocomplex
PAE3173 Conserved hypothetical 3 1 (130)
PAE3144 Conserved hypothetical 4 1 (116)
PAE2072 Conserved protein 5 1 (120) Potential heterocomplex
PAE2576 Hypothetical protein 6 5 (29, 33, 67, 143, 177) Potential heterocomplex
PAE2254 Hypothetical protein 7 2 (145, 154)
PAE3406 Conserved hypothetical 8 3 (40, 133, 147)
PAE0797 Short chain dehydrogenase 9 1 (259) Homodimer
PAE2075 Nitrilase, conjectural 10 2 (141, 257) Homodimer (257–257′)
PAE1689 Citrate synthase 11 2 (19, 394) Homodimer (19, 394)
PAE2310 Proline dehydrogenase 12 1 (408)
PAE0210 Conserved hypothetical 13 6 (75, 100, 107, 201, 265, 292) Intramolecular
PAE2489 Acetyl-CoA acyltransferase-associated 14 6 (58, 61, 72, 75, 137, 173) Intramolecular
PAE2701 Conserved hypothetical 15 2 (89, 114) Intramolecular
PAE3161 Hypothetical protein 16 4 (23, 25, 106, 138) Intramolecular

See Figure 1A for corresponding spot numbers. Cysteine residue numbers are given in parenthesis.

#

Complexes were assigned as likely homomeric vs. heteromeric based on spot positions in the gel and the presence or absence of likely partners related vertically. Where possible, assignment of likely disulfide connectivity was based on analysis of conservation in multiple sequence alignments, with conserved cysteines presumed to be functionally active rather than disulfide bonded.