Analysis of post-translational modifications of proteins by accurate mass measurement in fast atom bombardment mass spectrometry

Takao, Toshifumi; Yoshino, Ken‐ichi; Suzuki, Norio; Shimonishi, Yasutsugu

doi:10.1002/bms.1200191109

Cited by 16 publications

(4 citation statements)

References 27 publications

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“…Mass spectrometry has been used as a major tool for the high‐sensitivity detection and structural analysis of post‐translational modifications 12, 13. Examples include a phosphorylated amino acid (pSer, pThr, pTyr),14 a glycosylated amino acid (Ser, Thr, Asn),15 an oxidized Met,16 an acetyl‐Lys,17 ε ‐ N ‐methylated Lys,18 ε ‐ N,N,N ‐trimethylated Lys,19 etc.…”

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confidence: 99%

Top‐down analysis of protein isoprenylation by electrospray ionization hybrid quadrupole time‐of‐flight tandem mass spectrometry; the mouse Tγ protein

Kassai

Satomi

Fukada

et al. 2004

Rapid Comm Mass Spectrometry

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Protein isoprenylation, an important post-translational modification with a lipid, involves the selective attachment of two types of isoprenoids, farnesyl (C15) and geranylgeranyl (C20). The isoprenoid is linked via a thioether bond to the C-terminal cysteine residue of a variety of cellular proteins, including the heterotrimeric G protein gamma-subunits. One member of the G protein family, transducin (Talpha/Tbetagamma), plays a central role in visual transduction, and the structure-function relationship has been extensively studied with purified proteins, predominantly with bovine transducin that was shown to be farnesylated at the C-terminal cysteine residue of the gamma-subunit (Tgamma). We report here the structure of the C-terminal modification of mouse Tgamma, which has not yet been elucidated owing to the low amount of protein that can be isolated from the mouse retina. Electrospray ionization mass spectrometry (ESI-MS) of the high-performance liquid chromatography (HPLC)-purified Tgamma was in good agreement with the calculated mass of the farnesylated and methylated form of mouse Tgamma (Pro1-Cys70). A 'top-down' analysis of intact Tgamma using an ESI hybrid quadrupole time-of-flight (TOF) tandem mass spectrometer provided isoprenyl-specific ions that were observed to produce ions separated by 204 Da from the conventional (unmodified) precursor ion or the C-terminal sequence ions. Such characteristic fragmentation on an isoprenoid observed in top-down analysis could be useful in general for determining the type of isoprenylation as well as probing the site of modification in the protein sequence.

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confidence: 99%

Top‐down analysis of protein isoprenylation by electrospray ionization hybrid quadrupole time‐of‐flight tandem mass spectrometry; the mouse Tγ protein

Kassai

Satomi

Fukada

et al. 2004

Rapid Comm Mass Spectrometry

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“…(CAS Registry Numbers are copyrighted by the American Chemical Society and used with permission of the Chemical Abstracts Service of the American Chemical Society.) The RESID Database provides a means for calculating both chemical-average and monoisotopic molecular weights for modified peptides in order to facilitate their identification by mass-spectroscopy (3,4). Structural diagrams are presented in GIF format, and molecular models in PDB format are provided for use with widely available WWW display programs such as RasMol (5).…”

Section: Database Descriptionmentioning

confidence: 99%

The RESID Database of protein structure modifications: 2000 update

Garavelli¹

2000

Nucleic Acids Research

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The RESID Database contains supplemental information on post-translational modifications for the standardized annotations appearing in the PIR-International Protein Sequence Database. The RESID Database includes: systematic and frequently observed alternate names, Chemical s Service registry numbers, atomic formulas and weights, enzyme activities, indicators for N-terminal, C-terminal or peptide chain cross-link modifications, keywords, literature citations with database cross-references, structural diagrams and molecular models. Since 1995 updates of the RESID Database have appeared as often as weekly, and full releases appear quarterly. The database is freely accessible through the PIR Web site http://pir.georgetown.edu/pirwww/dbinfo/resid.html and by FTP.

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“…(CAS Registry Numbers are copyrighted by the American Chemical Society and used with permission of the Chemical Abstracts Service of the American Chemical Society.) The RESID Database provides a means for calculating both chemicalaverage and monoisotopic molecular weights for modified peptides in order to facilitate their identification by mass-spectroscopy (3,4). Release 16.00 contains over 250 entries describing features annotated in the Protein Sequence Database.…”

Section: Database Descriptionmentioning

confidence: 99%

The RESID Database of protein structure modifications

Garavelli

1999

Nucleic Acids Research

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Because the number of post-translational modifications requiring standardized annotation in the PIR-International Protein Sequence Database was large and steadily increasing, a database of protein structure modifications was constructed in 1993 to assist in producing appropriate feature annotations for covalent binding sites, modified sites and cross-links. In 1995 RESID was publicly released as a PIR-International text database distributed on CD-ROM and accessible through the ATLAS program. In 1998 it was made available on the PIR Web site at http://www-nbrf.georgetown.edu/pir/searchdb++ +.html . The RESID Database includes such information as: systematic and frequently observed alternate names; Chemical s Service registry numbers; atomic formulas and weights; enzyme activities; indicators forN-terminal, C-terminal or peptide chain cross-link modifications; keywords; and literature citations with database cross-references. The RESID Database can be used to predict atomic masses for peptides, and is being enhanced to provide molecular structures for graphical presentation on the PIR Web site using widely available molecular viewing programs.

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Analysis of post-translational modifications of proteins by accurate mass measurement in fast atom bombardment mass spectrometry

Cited by 16 publications

References 27 publications

Top‐down analysis of protein isoprenylation by electrospray ionization hybrid quadrupole time‐of‐flight tandem mass spectrometry; the mouse Tγ protein

Top‐down analysis of protein isoprenylation by electrospray ionization hybrid quadrupole time‐of‐flight tandem mass spectrometry; the mouse Tγ protein

The RESID Database of protein structure modifications: 2000 update

The RESID Database of protein structure modifications

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