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103. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins

Author

Verhagen, Anne M., Ekert, Paul G., Pakusch, Miha, Silke, John, Connolly, Lisa M., Reid, Gavin E., Moritz, Robert L., Simpson, Richard J., and Vaux, David L.

Subjects
Cytochemistry -- Research, Mammals -- Genetic aspects, Carrier proteins -- Physiological aspects, Biological sciences
Abstract

A novel mammalian protein that may promote apoptosis by binding to and antagonizing IAP proteins has been identified. It is called DIABLO for 'direct IAP-binding protein with low pl.' Coimmunoprecipitation and 2D immobilized pH gradient/SDS PAGE was used, followed by electrospray ionization tandem mass spectrometry.

Published
2000

109. sj-pdf-1-ems-10.1177_1469066720960341 - Supplemental material for Shedding light on isomeric FAHFA lipid structures using 213 nm ultraviolet photodissociation mass spectrometry

Author

Buenger, Edgar White and Reid, Gavin E

Subjects
FOS: Materials engineering, 91299 Materials Engineering not elsewhere classified
Abstract

Supplemental material, sj-pdf-1-ems-10.1177_1469066720960341 for Shedding light on isomeric FAHFA lipid structures using 213 nm ultraviolet photodissociation mass spectrometry by Edgar White Buenger and Gavin E Reid in European Journal of Mass Spectrometry

Published
2020
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111. MPSA short communications

Author

Barnes, Jr., Eugene M., Calkin, Patricia A., Kuroda, Satoshi, Norioka, Shigemi, Mitta, Masanori, Kato, Ikunoshin, Sakiyama, Fumio, Nika, Heinz, Chow, David T., Hess, Daniel, Bures, Edward J., Morrison, Hamish D., Aebersold, Ruedi, Clore, G. Marius, Gronenborn, Angela M., Persson, Bengt, Argos, Patrick, James, Peter, Cannons, Andrew C., Solomonson, Larry P., Dombrowski, Kenneth E., Moddeman, William E., Wright, Stephen E., Barker, Winona C., George, David G., Mattagajasingh, Subhendra N., Misra, Hara P., Huang, Shuan Shian, Huang, Jung San, Lee, Y. C., Fischer, Wolfgang H., Craig, A. Grey, McFadden, Philip N., Lind-quist, Jonathan A., Bartlet-Jones, M., Jeffery, W., Hansen, H. F., Pappin, D. J. C., Bergman, Tomas, Hjelmqvist, Lars, Estonius, Mats, Jörnvall, Hans, Dorow, Donna S., Tschesche, H., Knäuper, V., Kleine, T., Reinemer, P., Schnierer, S., Grams, F., Bode, W., Southan, Christopher, Fantom, Kenneth, Lavery, Patric, Findlay, J. B. C., Akrigg, D., Attwood, T. K., Beck, M. J., Bleasby, A. J., North, A. C. T., Parry-Smith, D. J., Perkins, D. N., Aitken, A., Patel, Y., Martin, H., Jones, D., Robinson, K., Madrazo, J., Howell, S., Aebersold, Ruedi, Hess, Daniel, Yungwirth, Tom, Affolter, Michael, Amankwa, Lawrence, Hess, Daniel, Aebersold, Ruedi, Scheraga, Harold A., Yang, Chao -Yuh, Valentinova, Natalia V., Yang, Manlan, Gu, Zi -Wei, Gotto, Jr., Antonio M., Dovichi, Norman J., Waldron, Karen C., Chen, Min, Ireland, Ian, Omori, Akira, Yoshida, Sachiyo, Schaller, Johann, Lengweiler, Stephan, Rickli, Egon E., Bubis, José, Ortiz, Julio O., Möller, Carolina, Millán, Enrique J., Boyd, Victoria L., Bozzini, MeriLisa, Zhao, Jindong, DeFranco, Robert J., Yuan, Pau -Miau, Loudon, G. Marc, Nguyen, Duy, Kamo, Masaharu, Kawakami, Takao, Miyatake, Norifumi, Tsugita, Akira, Tsugita, Akira, Kamo, Masaharu, Takamoto, Keiji, Satake, Kazuo, Bischof, Oliver, Hechenberger, Mirko, Thiede, Bernd, Kruft, Volker, Wittmann-Liebold, Brigitte, Otto, Albrecht, Benndorf, Rainer, Wittmann-Liebold, Brigitte, Jungblut, Peter, Ühlein, Monika, Wittmann-Liebold, Brigitte, Urlaub, Henning, Kruft, Volker, Wittmann-Liebold, Brigitte, Berhardt, Rita, Kraft, Regine, Uhlmann, Heike, Beckert, Vita, Akizawa, Toshifumi, Ayabe, Takaaki, Matsukawa, Motomi, Itoh, Michiyasu, Nishi, Masatoshi, Sato, Hiroshi, Seiki, Motoharu, Yoshioka, Masanori, Lebl, Michal, Krchňák, Viktor, Sepetov, Nikolai F., Kočiš, Petr, Pátek, Marcel, Flegelová, Zuzana, Ferguson, Ronald, Lam, Kit S., Moritz, Robert L., Eddes, James, Ji, Hong, Reid, Gavin E., Simpson, Richard J., Seffens, William, Poulter, C. Dale, Dolence, Julia M., Bond, Pamela D., Nokihara, Kiyoshi, Ikegaya, Kazuo, Morita, Naoki, Ohmura, Takao, Salikhov, S. I., Sagdiev, N. J., Korneev, A. S., Dolimbek, Behzod Z., Atassi, M. Zhouhair, Rosenberg, J. S., Yun, Z., Wyde, P. R., Atassi, M. Z., Gaskell, Simon J., Anumula, Kalyan Rao, Goldenberg, David P., Appella, Ettore, Fiscella, Michelle, Zambrano, Nicola, Ullrich, Stephen J., Sakaguchi, Kazuyasu, Sakamoto, Hiroshi, Lewis, Marc S., Lin, David, Mercer, W. Edward, Anderson, Carl W., Anderson, Carl W., Connelly, Marjorie A., Zhang, Hong, Sipley, John D., Lees-Miller, Susan P., Sakaguchi, Kazuyasu, Ullrich, Stephen J., Jackson, Stephen P., Appella, Ettore, Xie, Yong-hong, Yang, Manlan, Quion, Jun A., Gotto, Jr., Antonio M., Yang, Chao-yuh, Brandt, W. F., Alk, H., Bhaskaran, R., Yu, Chin, Yang, C. C., Henschen, Agnes H., Ashman, Keith, Mann, Matthias, Guevara, Jr., Juan, Nguyen, Hung Michael, Davison, Daniel B., Morrisett, Joel D., Perham, Richard N., Marvin, Donald A., Symmons, Martyn F., Terry, Tamsin D., Beg, Z. H., Stonik, J. A., Hoeg, J. M., Brewer, Jr., H. B., Gorovits, Boris M., Raman, C. S., and Horowtiz, Paul M.

Published
1994
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112. MPSA abstracts

Author

Aminlari, Mahmoud, Asquith, Thomas, Sarlo, Katherine, Bailey, Jerome M., Tu, Oanh, Issai, Gilbert, Ha, Alice, Shively, John E., Bell, Alexander W., Baur, Nicole C., Bergeron, John J. M., Ou, Wei -Jia, Thomas, David Y., Cianflone, Katherine, Baldo, Allain, Hincke, Maxwell T., Momparler, Richard L., Laliberté, Josée, Thomson, David M. P., Sutherland, M., Besada, Vladimir, Gonzalez, Javier, Padron, Gabriel, Garay, Hilda, Reyes, Osvaldo, Takao, Toshifumi, Shimonishi, Yasutsugu, Bischoff, Rainer, Roecklin, Dominique, Bouchon, Bernadette, Klarskov, Klaus, Van Dorsselaer, Alain, Brake, Patricia G., Pacitti, Anne, Higgins, Terry, Stevis, Panos, Malinowski, John, McElhiney, Sue, Huang, Janes, Vestal, Christine, Buckel, Scott D., Stevenson, Tracy, Loo, Joseph A., Caffrey, Martin, Wang, Jin, Wallace, Carmichael J. A., Clark-Lewis, Ian, Carraway, C. A. Carothers, Huang, J., Li, Y., Juang, S. -H., Gallo, A., Mayer, B. J., Carraway, K. L., Coleman, Patrick L., Sarpong, Daniel, Deerfield, II, David W., Holland-Minkley, Amanda, Hempel, John D., Nicholas, Jr., Hugh B., Denslow, Nancy D., Folmar, Leroy C., Sullivan, Craig V., Dixon, James D., Mark, Jonathan P., Elicone, Christopher P., Maleknia, Simin D., McGuinness, Brian F., Regnier, Fred E., Afeyan, Noubar B., Dolence, Julia M., Poulter, C. Dale, Egorov, Tsezi, Musolyamov, Alexander, Popineau, Yves, Andersen, Jens, Roepstorff, Peter, Falkenstein, Roberto J., Biscoglio de Jiménez Bonino, Mirtha J., Peña, Clara, Gauggel, D. L., Asquith, T. N., Isfort, R. J., Miller, N. S., Cody, D. B., Giblin, Michael F., Wong, Tuck C., Quinn, Thomas P., Grant, Gregory A., Crankshaw, Mark W., Griffith, Scott, Schroeder, Steve, Quinn, Thomas, Guinet, F., Petillot, Y., Chapsal, J. M., Dubayle, J., Greco, F., Barge, O., Forest, E., Valentin, C., Hahn, Frederick M, Baker, Jonathan A., Poulter, C. Dale, Haniu, Mitsuru, Kenney, William C., Rohde, Michael F., Harman, James G., Lee, Eun Ju, Glasgow, Joel, Lew, Sew Fen, Belduz, Ali O., Harris, Reed J., Molony, Michael S., Keyt, Lene H., Wu, Shiaw -Lin, Hawke, David H., Tso, Jaqueline, Early, Sherrell, Miller, Chad G., Hayman, G. Thomas, Miernyk, Jan A., Hellman, Ulf, Wernstedt, Christer, Góñez, Jorge, Hess, Daniel, Studer, Ralph, Hunziker, Peter E., Hirano, Hisashi, Watanabe, Yoshihiro, Barbashov, Sergei F., Komatsu, Setsuko, Hemmings, Andrew M., Miyagi, Masaru, Tsunasawa, Susumu, Huber, Reuben E., Roth, Nathan J., Gaunt, Michael T., Jenö, Paul, Mini, Thierry, Moes, Suzette, Horst, Martin, Jinnai, Kenji, Ashizawa, Tetsuo, Atassi, M. Zouhair, Johnsen, Anders H., Jensen, Hanne, Rehfeld, Jens F., Kamo, Masaharu, Kawakami, Takao, Miyatake, Norifumi, Tsugita, Akira, Keen, JN, Zagalsky, PF, Findlay, JBC, Kraft, Regine, Kostka, Susanne, Hartmann, Enno, Krutzsch, Henry C., Inman, John K., Machalinski, Claudia, Bonino, Mirtha Biscoglio de Jiménez, McRorie, Donald K., Dieckmann, Gregg R., Heilman, Susan, DeGrado, William F., Pecoraro, Vincent L., Kenny, James, Sahakian, Julie, Tso, Jacqueline, Moyer, Mary B., Burkhart, William A., Muranova, Tatyana, Makova, Lubov, Nicholas, Hugh, Hempel, John, Hinich, Amy, Deerfield, David, Behrmann, Joseph, Ropelewski, Alex, Nixon, Lori, Maneri, Leonard, Nugent, Kerry, Stoney, Ken, Wieser, John, Ohguro, Hiroshi, Palczewski, Krzysztof, Walsh, Kenneth A., Johnson, Richard S., Packman, Leonard C, Webster, Carl, Gray, John, Padrón, G., Morera, V., González, L. J., Támbara, Y., Besada, V., Villalonga, R., Chinea, G., Reyes, O., Bringas, H. Garay R., Nazábal, C., Parkinson, Bruce P., Yamada, Kent A., Randolph, Anne, Pisano, Anthony, Packer, Nicole H., Redmond, John W., Williams, Keith L., Gooley, Andrew A., Rasmussen, Hanne H., Mørtz, Ejvind, Mann, Matthias, Celis, Julio E., Rasmussen, Lone K., Sørensen, Esben S., Petersen, Torben E., Gliemann, Jørgen, Jensen, Poul Henning, Renlund, Staffan, Wadensten, Henrik, Persson, Annika, Persson, Per, Johansson, Agneta, Edlund, Per -Olof, Rose, Donald J., Sack, Ragna, Apffel, Alex, Miller, Chad, Levine, Rodney L., Sakaguchi, Kazuyasu, Zambrano, Nicola, Lewis, Marc S., Baldwin, Eric T., Shapiro, Bruce A., Erickson, John W, Omichinski, James G., Clore, G. Marius, Gronenborn, Angela M., Appella, Ettore, Schröder, Werner, Moser, Irmgard, Pansegrau, Werner, Lanka, Erich, Simpson, Richard J., Eddes, James, Ji, Hong, Reid, Gavin E., Moritz, Robert L., Højrup, Peter, Speicher, David W., Reim, David F., Speicher, Kaye D., Srinivasa, B. R., Barde, S. P., Stirtan, William G., Sukhanova, Alyona, Vorob'ev, Sergey, Gabibov, Alexander, Bronstein, Igor, Tanaka, Kenji, Einaga, Kuniko, Tsukada, Minoru, Tait, Jonathan F., Fujikawa, Kazuo, Takamoto, Keiji, Satake, Kazuo, Vakser, Ilya A., Velikodvorskaia, V. V., Gabibov, A. G., Rabinkov, A. G., Videler, Tennie, Osborne, Michael, Moore, Geoffrey, James, Richard, Kleanthous, Colin, Walent, Jane H., Bessen, Richard, Marsh, Dick, Clore, G. Marius, Niece, Ronald L., Tsao, Francis H. C., Wang, Hong, Weinberger, Scot R., Chakel, Lynn M., Wondrak, Ewald M., Kimmel, Alan R., and Louis, John M.

Published
1994
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113. Solution structure of a polypeptide containing four heptad repeat units from a Merozoite surface antigen of Plasmodium falciparum

Author

Mulhern, Terrence D., Howlett, Geoffrey J., Reid, Gavin E., Simpson, Richard J., McColl, Damian J., Anders, Robin F., and Norton, Raymond S.

Subjects
Plasmodium falciparum -- Research, Parasite antigens -- Research, Molecular structure -- Analysis, Biological sciences, Chemistry
Abstract

NMR analysis of the solution structure of a 38-residue polypeptide containing four heptad repeat units from a merozoite surface antigen, SPAM-H1, of Plasmodium falciparum suggests that the monomeric peptide contains a bent alpha-helix extending from Ser10 to Lys32. Slowly exchanging amide protons are present in the vicinity of the C-terminus and the last two turns of the helix. A C-capping motif accounts for the stability of the C-terminus by involving the side chain of an asparagine in a position external to the C-cap residue.

Published
1995

127. Huntingtin Inclusions Trigger Cellular Quiescence, Deactivate Apoptosis, and Lead to Delayed Necrosis

Author

Ramdzan, Yasmin M., Trubetskov, Mikhail M., Ormsby, Angelique R., Newcombe, Estella A., Sui, Xiaojing, Tobin, Mark J., Bongiovanni, Marie N., Gras, Sally L., Dewson, Grant, Miller, Jason M.L., Finkbeiner, Steven, Moily, Nagaraj S., Niclis, Jonathan, Parish, Clare L., Purcell, Anthony W., Baker, Michael J., Wilce, Jacqueline A., Waris, Saboora, Stojanovski, Diana, Böcking, Till, Ang, Ching-Seng, Ascher, David B., Reid, Gavin E., and Hatters, Danny M.

Published
2017
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132. A biosensor-based framework to measure latent proteostasis capacity

Author

Wood, Rebecca J., Ormsby, Angelique R., Radwan, Mona, Cox, Dezerae, Sharma, Abhishek, Vöpel, Tobias, Ebbinghaus, Simon, Oliveberg, Mikael, Reid, Gavin E., Dickson, Alex, Hatters, Danny M., Wood, Rebecca J., Ormsby, Angelique R., Radwan, Mona, Cox, Dezerae, Sharma, Abhishek, Vöpel, Tobias, Ebbinghaus, Simon, Oliveberg, Mikael, Reid, Gavin E., Dickson, Alex, and Hatters, Danny M.

Abstract

The pool of quality control proteins (QC) that maintains protein-folding homeostasis (proteostasis) is dynamic but can become depleted in human disease. A challenge has been in quantitatively defining the depth of the QC pool. With a new biosensor, flow cytometrybased methods and mathematical modeling we measure the QC capacity to act as holdases and suppress biosensor aggregation. The biosensor system comprises a series of barnase kernels with differing folding stability that engage primarily with HSP70 and HSP90 family proteins. Conditions of proteostasis stimulation and stress alter QC holdase activity and aggregation rates. The method reveals the HSP70 chaperone cycle to be rate limited by HSP70 holdase activity under normal conditions, but this is overcome by increasing levels of the BAG1 nucleotide exchange factor to HSPA1A or activation of the heat shock gene cluster by HSF1 overexpression. This scheme opens new paths for biosensors of disease and proteostasis systems.

Published
2018
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137. Femtosecond laser-induced ionization/dissociation of protonated peptides

Author

Kalcic, Christine L., Gunaratne, Tissa C., Jones, A. Daniel, Dantus, Marcos, and Reid, Gavin E.

Subjects
Ionization -- Analysis, Mass spectrometry -- Usage, Peptides -- Chemical properties, Peptides -- Structure, Laser pulses, Ultrashort -- Usage, Chemistry
Abstract

The implementation and results from a novel strategy for peptide sequence and modification analysis (femtosecond laser-induced ionization/dissociation (fs-LID)) involving the use of ultrashort laser pulses for energy deposition and nonergodic dissociation in a quadrupole ion trap mass spectrometer are presented. The studies have shown that fs-LID is a viable alternate ion activation strategy for peptide sequence and modification analysis.

Published
2009

138. Energetics and dynamics of the fragmentation reactions of protonated peptides containing methionine sulfoxide or aspartic acid via energy- and time-resolved surface induced dissociation

Author

Hadi Lioe, Laskin, Julia, Reid, Gavin E., and O'Hair, Richard A.J.

Subjects
Entropy (Physics) -- Analysis, Fourier transform infrared spectroscopy -- Analysis, Methionine -- Structure, Methionine -- Chemical properties, Methionine -- Thermal properties, Chemicals, plastics and rubber industries
Abstract

The surface-induced dissociation (SID) is used to explain the energetics and dynamics of the fragmentation reactions of various protonated peptides containing methionine sulfoxide or aspartic acid. These gas phase reactions are found to be governed mainly by the entropic effects.

Published
2007

139. A point mutation converts dihydroneopterin aldolase to a cofactor-independent oxygenase

Author

Yi Wang, Scherperel, Gwynyth, Roberts, Kade D., Jones, A. Daniel, Reid, Gavin E., and Honggao Yan

Subjects
Binding sites (Biochemistry) -- Research, Fructosediphosphate aldolase -- Structure, Fructosediphosphate aldolase -- Chemical properties, Chemistry
Abstract

A study demonstrates that dihydroneopterin aldolase (DHNA) catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the folate biosynthetic pathway. The conserved tyrosine residue plays only a minor role in the formation of the enol reaction intermediate but a critical role in the protonation of the enol intermediate to form 6-hydroxymethyl-7,8-dihydropterin.

Published
2006

140. A biosensor-based framework to measure latent proteostasis capacity

Author

Wood, Rebecca J., primary, Ormsby, Angelique R., additional, Radwan, Mona, additional, Cox, Dezerae, additional, Sharma, Abhishek, additional, Vöpel, Tobias, additional, Ebbinghaus, Simon, additional, Oliveberg, Mikael, additional, Reid, Gavin E., additional, Dickson, Alex, additional, and Hatters, Danny M., additional

Published
2018
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144. A thiol probe for measuring unfolded protein load and proteostasis in cells

Author

Chen, Moore Z., primary, Moily, Nagaraj S., additional, Bridgford, Jessica L., additional, Wood, Rebecca J., additional, Radwan, Mona, additional, Smith, Trevor A., additional, Song, Zhegang, additional, Tang, Ben Zhong, additional, Tilley, Leann, additional, Xu, Xiaohong, additional, Reid, Gavin E., additional, Pouladi, Mahmoud A., additional, Hong, Yuning, additional, and Hatters, Danny M., additional

Published
2017
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145. Arginine in C9ORF72Dipolypeptides Mediates Promiscuous Proteome Binding and Multiple Modes of Toxicity*

Author

Radwan, Mona, Ang, Ching-Seng, Ormsby, Angelique R., Cox, Dezerae, Daly, James C., Reid, Gavin E., and Hatters, Danny M.

Abstract

C9ORF72-associated Motor Neuron Disease patients feature abnormal expression of 5 dipeptide repeat (DPR) polymers. We found the most toxic DPRs, PR and GR, were particularly promiscuous binders to endogenous proteins. This included ribosomal proteins, translation initiation factors and translation elongation factors. The corresponding biological impacts were multipronged and included stalling of ribosomes during translation, hypomethylation of endogenous proteins, and the destabilization of the actin cytoskeleton. The findings point to new mechanisms of toxicity in disease caused by arg-rich DPRs.

Published
2020
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146. Widespread remodeling of proteome solubility in response to different protein homeostasis stresses.

Author

Xiaojing Sui, Pires, Douglas E. V., Ormsby, Angelique R., Cox, Dezerae, Shuai Nie, Vecchi, Giulia, Vendruscolo, Michele, Ascher, David B., Reid, Gavin E., and Hatters, Danny M.

Subjects
HEAT shock proteins, HUNTINGTON disease, PROTEIN folding, SOLUBILITY, PROTEIN stability
Abstract

The accumulation of protein deposits in neurodegenerative diseases has been hypothesized to depend on a metastable subproteome vulnerable to aggregation. To investigate this phenomenon and the mechanisms that regulate it, we measured the solubility of the proteome in the mouse Neuro2a cell line under six different protein homeostasis stresses: 1) Huntington's disease proteotoxicity, 2) Hsp70, 3) Hsp90, 4) proteasome, 5) endoplasmic reticulum (ER)-mediated folding inhibition, and 6) oxidative stress. Overall, we found that about one-fifth of the proteome changed solubility with almost all of the increases in insolubility were counteracted by increases in solubility of other proteins. Each stress directed a highly specific pattern of change, which reflected the remodeling of protein complexes involved in adaptation to perturbation, most notably, stress granule (SG) proteins, which responded differently to different stresses. These results indicate that the protein homeostasis system is organized in a modular manner and aggregation patterns were not correlated with protein folding stability (ΔG). Instead, distinct cellular mechanisms regulate assembly patterns of multiple classes of protein complexes under different stress conditions. [ABSTRACT FROM AUTHOR]

Published
2020
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147. A Thiol Probe for Measuring Unfolded Protein Load and Proteostasis in Cells

Author

Chen, Moore Z., Moily, Nagaraj S., Bridgford, Jessica L., Wood, Rebecca J., Radwan, Mona, Smith, Trevor A., Song, Zhegang, Tang, Ben Zhong, Tilley, Leann, Xu, Xiaohong, Reid, Gavin E., Pouladi, Mahmoud A., Hong, Yuning, Hatters, Danny M., Chen, Moore Z., Moily, Nagaraj S., Bridgford, Jessica L., Wood, Rebecca J., Radwan, Mona, Smith, Trevor A., Song, Zhegang, Tang, Ben Zhong, Tilley, Leann, Xu, Xiaohong, Reid, Gavin E., Pouladi, Mahmoud A., Hong, Yuning, and Hatters, Danny M.

Abstract

When proteostasis becomes unbalanced, unfolded proteins can accumulate and aggregate. Here we report that the dye, tetraphenylethene maleimide (TPE-MI) can be used to measure cellular unfolded protein load. TPE-MI fluorescence is activated upon labelling free cysteine thiols, normally buried in the core of globular proteins that are exposed upon unfolding. Crucially TPE-MI does not become fluorescent when conjugated to soluble glutathione. We find that TPE-MI fluorescence is enhanced upon reaction with cellular proteomes under conditions promoting accumulation of unfolded proteins. TPE-MI reactivity can be used to track which proteins expose more cysteine residues under stress through proteomic analysis. We show that TPE-MI can report imbalances in proteostasis in induced pluripotent stem cell models of Huntington disease, as well as cells transfected with mutant Huntington exon 1 before the formation of visible aggregates. TPE-MI also detects protein damage following dihydroartemisinin treatment of the malaria parasites Plasmodium falciparum. TPE-MI therefore holds promise as a tool to probe proteostasis mechanisms in disease. © 2017 The Author(s).

Published
2017

148. Charge-State-Dependent Sequence Analysis of Protonated Ubiquitin Ions via Ion Trap Tandem Mass Spectrometry

Author

Reid, Gavin E., Wu, Jin, Chrisman, Paul A., Wells, J. Mitchell, and McLuckey, Scott A.

Subjects
Proteins -- Research, Mass spectrometry -- Usage, Ubiquitin -- Research, Chemistry
Abstract

One of the major factors governing the 'top-down' sequence analysis of intact multiply protonated proteins by tandem mass spectrometry is the effect of the precursor ion charge state on the formation of product ions. To more fully understand this effect, electrospray ionization coupled to a quadrupole ion trap mass spectrometer, collision-induced dissociation, and gas-phase ion/ion reactions have been employed to examine the fragmentation of the [[M + 12H].sup.12] + to [M + H]+ ions of bovine ubiquitin. At low charge states (+1 to +6), loss of [NH.sub.3] or [H.sub.2]O from the protonated precursor and directed cleavage at aspartic acid residues was observed. At intermediate charge states, (+7, +8, and +9), extensive nonspecific fragmentation of the protein backbone was observed, with 50% sequence coverage obtained from the [[M + 8H].sup.8+] ion alone. At high charge states, (+10, +11, +12), the single dominant channel that was observed was the preferential fragmentation of a single proline residue. These data can be readily explained in terms of the current model for intramolecular proton mobilization, that is, the 'mobile proton model', the mechanisms for amide bond dissociation developed for protonated peptides, as well as the structures of the multiply charged ions of ubiquitin in the gas phase, examined by ion mobility and hydrogen/deuterium exchange measurements.

Published
2001

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