Table 1. Interprotein Cross-Linked Peptides from Proteins Involved in Transcription and Translation.
mass (Da) | sequence peptide A | Uniprot entry name | position XL residue | sequence peptide B | Uniprot entry name | position XL residue | (template) PDB file model | distance (Å) in structure model |
---|---|---|---|---|---|---|---|---|
1788.0 | XSLEEVK | RPOA | 294 | XSLEEVK | RPOA | 294 | n.a. | |
2194.2 | IXELGPR | RSPB | 112 | DTXLGPEEITR | RPOB | 803 | n.a. | |
2298.2 | MYLXEIGR | SIGA | 107 | QLLSEXEYR | RPOC | 153 | 4IGC | 16.1 |
2527.4 | LLTVXIPVR | GUDB | 52 | XDVVDEVYDQR | NUSA | 62 | n.a. | |
2629.4 | IGAEVXDGDLLVGK | RPOB | 837 | GYTPADANXR | RPOA | 155 | 2O5I$ | 12.3 |
2672.5 | XLALK | RPOA | 84 | VAVAANSLXNVTFTEEQR | RPOC | 545 | 2O5I$ | 20.0 |
2762.5 | AQEXVFPMTAEGK | GREA | 5 | XGFTATVIPNR | RPOB | 156 | 4WQT | n.a. |
2974.6 | DTXLGPEEITR | RPOB | 803 | TLXPEKDGLFCER | RPOC | 40 | 2O5I$ | 12.7 |
3026.6 | XGFTATVIPNR | RPOB | 156 | DXQQEIVVQGAVETR | RPOC | 987 | 2O5I$ | 21.1 |
3066.7 | IAAQTAXQVVTQR | NUSA | 111 | VTPXGVTELTAEER | RPOB | 849 | n.a. | |
3387.6 | VTPXGVTELTAEER | RPOB | 849 | IFGPTXDWECHCGK | RPOC | 56 | 2O5I$ | 14.4 |
3510.8 | LVPAGTGMMXYR | RPOC | 1179 | ALEEIDAGLLSFEXEDRE | RPOZ | 63 | 2O5I$ | 13.8 |
3780.0 | XEELGDR | RPOE | 48 | VIDAGDTDVLPGTLLDIHQFTEANXK | RPOC | 1104 | n.a. | |
4572.3 | GILAKPLXEGTETIER | RPOC | 830 | SFGDLSENSEYDSAXEEQAFVEGR | GREA | 55 | 4WQT | 28.0 |
4695.7 | IGAEVXDGDLLVGK | RPOB | 837 | GYTPADANXRDDQPIGVIPIDSIYTPVSR | RPOA | 155 | 2O5I$ | 12.3 |
6461.1 | DTXLGPEEITR | RPOB | 803 | EILXIAQEPVSLETPIGEEDDSHLGDFIEDQEATSPSDHAAYELLK | SIGA | 258 | 4IGC | 11.6 |
1694.0 | VIXVVR | RL7 | 73 | GPXGELTR | RL6 | 31 | n.a. | |
1838.1 | XEVVQLK | RS2 | 132 | GEVLPTXK | RS3 | 210 | 3J9W | 22.3 |
1947.0 | DIIDXLK | RS13 | 62 | QXFASADGR | RL31 | 48 | n.a. | |
2083.2 | GXILPR | RS18 | 43 | SVSXTGTLQEAR | RS21 | 25 | n.a. | |
2217.2 | XFVSER | RS18 | 36 | IDPSXLELEER | RS5 | 8 | 3J9W | 86.2 |
2383.4 | XAVIER | RS6 | 20 | ILDQSAEXIVETAK | RS10 | 24 | 3J9W | 149.7 |
2392.3 | AEDVAXLR | RS5 | 155 | VFLXYGQNNER | RS8 | 65 | 3J9W | 12.4 |
2429.3 | XNEEGGK | RS3 | 212 | ILDQSAEXIVETAK | RS10 | 24 | 3J9W | <20.9* |
2433.3 | XFVSER | RS18 | 36 | ILDQSAEXIVETAK | RS10 | 24 | 3J9W | 116.1 |
2438.3 | GEVLPTXK | RS3 | 210 | VXVLDVNENEER | RS1H | 326 | n.a. | |
2457.3 | ILDQSAEXIVETAKR | RS10 | 24 | NEEGGX | RS3 | 218 | n.a. | |
2498.5 | XALNSLTGK | RS3 | 88 | VXVLDVNENEER | RS1H | 326 | n.a. | |
2500.3 | GIVTXVEDK | RS1H | 25 | QAQDSVXEEAQR | RS2 | 81 | n.a. | |
2539.4 | GEVLPTXK | RS3 | 210 | ILDQSAEXIVETAK | RS10 | 24 | 3J9W | 18.5 |
2557.4 | XKNEEGGK | RS3 | 211 | ILDQSAEXIVETAK | RS10 | 24 | 3J9W | 16.9 |
2571.4 | XALNSLTGK | RS3 | 88 | XQAQDSVKEEAQR | RS2 | 74 | 3J9W | 87.4 |
2654.4 | EITGLGLXEAK | RL7 | 84 | XAAGIESGSGEPNR | RL11 | 81 | n.a. | |
2701.6 | VVXVVK | RL11 | 7 | MLVITPYDXTAIGDIEK | RRF | 72 | n.a. | |
2725.4 | GPQAANVTXEA | CSPB | 65 | XQAQDSVKEEAQR | RS2 | 74 | n.a. | |
2728.5 | SVSXTGTLQEAR | RS21 | 25 | IDPSXLELEER | RS5 | 8 | n.a. | |
2733.4 | XNESLEDALR | RS21 | 8 | XLSEYGLQLQEK | RS4 | 43 | n.a. | |
2739.4 | YEVGEGIEXR | EFTS | 278 | AEVYVLSXEEGGR | EFTU | 316 | 1EFU | 18.6 |
2749.4 | ELVDNTPXPLK | RL7 | 95 | XAAGIESGSGEPNR | RL11 | 81 | n.a. | |
2845.5 | AXLSGTAERPR | RL18 | 21 | GGDDTLFAXIDGTVK | RL28 | 70 | n.a. | |
2861.5 | XNESLEDALR | RS21 | 8 | XKLSEYGLQLQEK | RS4 | 42 | n.a. | |
2881.5 | IDPSXLELEER | RS5 | 8 | VXVLSVDRDNER | RS1H | 240 | n.a. | |
2882.6 | IAXIEVVR | RL19 | 83 | XLLDYAEAGDNIGALLR | EFTU | 266 | n.a. | |
3080.6 | VHINILEIXR | RS3 | 106 | ELEETPXADQEDYR | RS1H | 349 | n.a. | |
3153.8 | EAXELVDNTPKPLK | RL7 | 87 | LALETGTAFIEXR | MTNK | 377 | n.a. | |
3184.7 | XQAQDSVKEEAQR | RS2 | 74 | ILDQSAEXIVETAK | RS10 | 24 | 3J9W | 75.4 |
3427.8 | EAXELVDNTPKPLK | RL7 | 87 | SLLGNMVEGVSXGFER | RL6 | 82 | n.a. | |
3524.8 | VNITIHTAXPGMVIGK | RS1 | 71 | ELEETPXADQEDYR | RS1H | 349 | n.a. | |
3789.9 | EAXELVDNTPKPLK | RL7 | 87 | AXEAEAAGADFVGDTDYINK | RL1 | 85 | n.a. |
X, cross-linked K residue; *, linked residue K212 (RS3) is not in structure model; distance is assumed based on a maximal distance of 4 Å between Cα atoms of K211 and K212; $, the structure of the RNAP elongation complex was modeled as described in the Experimental Procedures; n.a., model not available or linked residue not in structure. Uniprot entry names RPOA, RPOB, RPOC, RPOE, and RPOZ correspond to subunits α, β, β′, δ, and ω of RNAP.