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Research Article

Extensive Lysine Methylation in Hyperthermophilic Crenarchaea: Potential Implications for Protein Stability and Recombinant Enzymes

Table 1

Methylation sites identified in S. solfataricus RNA polymerase subunits.

ProteinSubunitResiduePeptide (methyllysine in bold)

1Sso0225 395KELASTLAPGYIIER
2Sso0225659KEIYNEIDR
3Sso0227 -C12IVEKTLYEMGVVPVEEVIR
4Sso0227311GYKGKEYYR
5Sso0227349FLQEFKELSPEQAKR
6Sso0071RpoD115DIKSEDPSVVPISGDIPIVLLGTNQK
7Sso0415 20IPPNEFGKPLNEIALNELR
8Sso0415131GIIFGEKSKKVIQKGDKVR
9Sso0415133GIIFGEKSKKVIQKGDKVR
10Sso0415171QPYLGKLEWITQTKK
11Sso0415179LEWITQTKK
12Sso0751RpoF54CDAESAQKVIEELSNIVSR
13Sso0751102TYTSEDIQKIIDIIR
14Sso5468RpoH30HEVLNIDEAYKILK
15Sso546868KSQLYGEVVSYR
16Sso5577RpoL71DALLKAIENIR
17Sso557788GMTSHYIDEIKGLTK
18Sso5865RpoP19TFTDEQLKVLPGVR
19Sso0396Rpo1366KLFEDNYK
20Sso039698KAKKAVSKKVKKTKKKEKSVEG
21Sso0396100KAKKAVSKKVKKTKKKEKSVEG

Monomethylated lysines are shown in bold. All lysines are conserved in the S. shibatae RNAP sequence with the exception of the lysine in peptide 19, which is an arginine in S. shibatae Rpo13.
Supplementary Table contains more detail and evidence supporting the identification of each modification site.

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