ProMoST (Protein Modification Screening Tool): a web-based tool for mapping protein modifications on two-dimensional gels

被引:84
作者
Halligan, BD
Ruotti, V
Jin, W
Laffoon, S
Twigger, SN
Dratz, EA
机构
[1] Med Coll Wisconsin, Bioinformat Res Ctr, Milwaukee, WI 53213 USA
[2] Med Coll Wisconsin, Biotechnol & Biomed Engn Ctr, Milwaukee, WI 53213 USA
[3] Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 USA
关键词
D O I
10.1093/nar/gkh356
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
ProMoST is a flexible web tool that calculates the effect of single or multiple posttranslational modifications (PTMs) on protein isoelectric point (pI) and molecular weight and displays the calculated patterns as two-dimensional (2D) gel images. PTMs of proteins control many biological regulatory and signaling mechanisms and 2D gel electrophoresis is able to resolve many PTM-induced isoforms, such as those due to phosphorylation, acetylation, deamination, alkylation, cysteine oxidation or tyrosine nitration. These modifications cause changes in the pI of the protein by adding, removing or changing titratable groups. Proteins differ widely in buffering capacity and pI and therefore the same PTMs may give rise to quite different patterns of pI shifts in different proteins. It is impossible by visual inspection of a pattern of spots on a gel to determine which modifications are most likely to be present. The patterns of PTM shifts for different proteins can be calculated and are often quite distinctive. The theoretical gel images produced by ProMoST can be compared to the experimental 2D gel results to implicate probable PTMs and focus efforts on more detailed study of modified proteins. ProMoST has been implemented as cgi script in Perl available on a WWW server at http://proteomics.mcw.edu/promost.
引用
收藏
页码:W638 / W644
页数:7
相关论文
共 31 条
[1]   Proteomic method identifies proteins nitrated in vivo during inflammatory challenge [J].
Aulak, KS ;
Miyagi, M ;
Yan, L ;
West, KA ;
Massillon, D ;
Crabb, JW ;
Stuehr, DJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (21) :12056-12061
[2]   ProteomeWeb: A web-based interface for the display and interrogation of proteomes [J].
Babnigg, G ;
Giometti, CS .
PROTEOMICS, 2003, 3 (05) :584-600
[3]   Absolute quantification of the G protein-coupled receptor rhodopsin by LC/MS/MS using proteolysis product peptides and synthetic peptide standards [J].
Barnidge, DR ;
Dratz, EA ;
Martin, T ;
Bonilla, LE ;
Moran, LB ;
Lindall, A .
ANALYTICAL CHEMISTRY, 2003, 75 (03) :445-451
[4]   THE FOCUSING POSITIONS OF POLYPEPTIDES IN IMMOBILIZED PH GRADIENTS CAN BE PREDICTED FROM THEIR AMINO-ACID-SEQUENCES [J].
BJELLQVIST, B ;
HUGHES, GJ ;
PASQUALI, C ;
PAQUET, N ;
RAVIER, F ;
SANCHEZ, JC ;
FRUTIGER, S ;
HOCHSTRASSER, D .
ELECTROPHORESIS, 1993, 14 (10) :1023-1031
[5]   REFERENCE POINTS FOR COMPARISONS OF 2-DIMENSIONAL MAPS OF PROTEINS FROM DIFFERENT HUMAN CELL-TYPES DEFINED IN A PH SCALE WHERE ISOELECTRIC POINTS CORRELATE WITH POLYPEPTIDE COMPOSITIONS [J].
BJELLQVIST, B ;
BASSE, B ;
OLSEN, E ;
CELIS, JE .
ELECTROPHORESIS, 1994, 15 (3-4) :529-539
[6]   Caspase activation [J].
Boatright, KM ;
Salvesen, GS .
PROTEASES AND THE REGULATION OF BIOLOGICAL PROCESSES, 2003, 70 :233-242
[8]   Regeneration of peroxiredoxins during recovery after oxidative stress - Only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress [J].
Chevallet, M ;
Wagner, E ;
Luche, S ;
van Dorsselaer, A ;
Leize-Wagner, E ;
Rabilloud, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (39) :37146-37153
[9]   Carboxyl methylation of Ras regulates membrane targeting and effector engagement [J].
Chiu, VK ;
Silletti, J ;
Dinsell, V ;
Wiener, H ;
Loukeris, K ;
Ou, GM ;
Philips, MR ;
Pillinger, MH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (08) :7346-7352
[10]   Phosphorylations of cyclin-dependent kinase 2 revisited using two-dimensional gel electrophoresis [J].
Coulonval, K ;
Bockstaele, L ;
Paternot, S ;
Roger, PP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (52) :52052-52060