TY - JOUR
T1 - Top-Down Proteomics Reveals Novel Protein Forms Expressed in Methanosarcina acetivorans
AU - Ferguson, Jonathan T.
AU - Wenger, Craig D.
AU - Metcalf, William W.
AU - Kelleher, Neil L.
N1 - Funding Information:
The authors are grateful to Dr. Gary Olsen for fruitful discussions, and Jun Kai Zhang for culturing M. acetivorans cells. N.L.K. acknowledges the National Institutes of Health (NIH GM 067193-06) and the University of Illinois Institute for Genomic Biology. W.W.M. acknowledges support in part by NSF MCB Division of Cellular and Biosciences grant no. MCB12466 and by DOE Energy Biosciences Program grant no. DEFG02-02-ER15296.
PY - 2009/9
Y1 - 2009/9
N2 - Using both automated nanospray and online liquid chromatography mass spectrometry LC-MS strategies, 99 proteins have been newly identified by top-down tandem mass spectrometry (MS/MS) in Methanosarcina acetivorans, the methanogen with the largest known genome [5.7 mega base pairs (Mb)] for an Archaeon. Because top-down MS/MS was used, 15 proteins were detected with mispredicted start sites along with an additional five from small open reading frames (SORFs). Beyond characterization of these more common discrepancies in genome annotation, one SORF resulted from a rare start codon (AUA) as the initiation site for translation of this protein. Also, a methylation on a 30S ribosomal protein (MA1259) was localized to Pro59-Val69, contrasting sharply from its homologue in Escherichia coli (rp S12) known to harbor an unusual β-thiomethylated aspartic acid residue.
AB - Using both automated nanospray and online liquid chromatography mass spectrometry LC-MS strategies, 99 proteins have been newly identified by top-down tandem mass spectrometry (MS/MS) in Methanosarcina acetivorans, the methanogen with the largest known genome [5.7 mega base pairs (Mb)] for an Archaeon. Because top-down MS/MS was used, 15 proteins were detected with mispredicted start sites along with an additional five from small open reading frames (SORFs). Beyond characterization of these more common discrepancies in genome annotation, one SORF resulted from a rare start codon (AUA) as the initiation site for translation of this protein. Also, a methylation on a 30S ribosomal protein (MA1259) was localized to Pro59-Val69, contrasting sharply from its homologue in Escherichia coli (rp S12) known to harbor an unusual β-thiomethylated aspartic acid residue.
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U2 - 10.1016/j.jasms.2009.05.014
DO - 10.1016/j.jasms.2009.05.014
M3 - Article
C2 - 19577935
AN - SCOPUS:69549109963
SN - 1044-0305
VL - 20
SP - 1743
EP - 1750
JO - Journal of the American Society for Mass Spectrometry
JF - Journal of the American Society for Mass Spectrometry
IS - 9
ER -