Biology:Protein stoichiometry
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Protein stoichiometry is analogous to chemical stoichiometry, from whence it derives its name.[1][2][3] In chemical stoichiometry, the number of atoms and their charge units are balanced on either side of a chemical rate equation. In protein stoichiometry, the proteins are balanced[4] according to Chargaff's rules.
In 1950, Chargaff published that the amounts of adenine and thymine in DNA were roughly or approximately the same, as were the amounts of cytosine and guanine.[5] This later became known as the first of Chargaff's rules. Because of this rule, relative units of mass are used to determine stoichiometry. Mass units can be counted under a microscope, or analysed with a spectrometer, which latter technique was first developed using isotope decoding by Cohen.
Chargaff's statement of his rules is as follows:[6]
- the sum of the purines (adenine and guanine) equals that of the pyrimidines (cytosine and thymine);
- the molar ratio of adenine to thymine equals 1;
- the molar ratio of guanine to cytosine equals 1.
And, as a direct consequence of the three last relationships,
- the number of 6–amino groups (adenine and cytosine) is the same as that of 6–keto groups (guanine and thymine).
How to
Several techniques for protein stoichiometry have been developed, amongst which:
- Absolute Quantification (AQUA)[7]
- Multiple Reaction Monitoring (MRM)[7]
- Fluorescence microscopy[8]
- Step-wise photobleaching of dye-labelled subunits (photobleaching)[9]
- hydrophobic photolabeling (HyPLa)[10]
- peptide-based mass spectrometry[11]
- proteomics-based mass spectrometry[12]
- cell fusion and single molecule imaging[13]
- isotope-coded mass spectrometry[14]
References
- ↑ Leake, Mark C.; Chandler, Jennifer H.; Wadhams, George H.; Bai, Fan; Berry, Richard M.; Armitage, Judith P. (2006). "Stoichiometry and turnover in single, functioning membrane protein complexes". Nature 443 (7109): 355–358. doi:10.1038/nature05135. PMID 16971952. Bibcode: 2006Natur.443..355L.
- ↑ Geng, Jiefei; Baba, Misuzu; Nair, Usha; Klionsky, Daniel J. (2008). "Quantitative analysis of autophagy-related protein stoichiometry by fluorescence microscopy". Journal of Cell Biology 182 (1): 129–140. doi:10.1083/jcb.200711112. PMID 18625846.
- ↑ De, Mrinmoy; Rana, Subinoy; Rotello, Vincent M. (2009). "Nickel-Ion-Mediated Control of the Stoichiometry of His-Tagged Protein/Nanoparticle Interactions". Macromolecular Bioscience 9 (2): 174–178. doi:10.1002/mabi.200800289. PMID 19127602.
- ↑ "Protein Structure Analysis with Mass Spectrometry". ThermoFisher Scientific. https://www.thermofisher.com/gu/en/home/industrial/mass-spectrometry/proteomics-protein-mass-spectrometry/proteomics-protein-mass-spectrometry-workflows/protein-structure-analysis-mass-spectrometry/protein-structure.html.
- ↑ Chargaff, Erwin; Stephen Zamenhof; Charlotte Green (May 1950). "Composition of human desoxypentose nucleic acid". Nature 165 (4202): 756–7. doi:10.1038/165756b0. PMID 15416834. Bibcode: 1950Natur.165..756C.
- ↑ Weintraub, Bob (September 2006). "Erwin Chargaff and Chargaff's Rules". Chemistry in Israel - Bulletin of the Israel Chemical Society (22): 29-31. https://drive.goo-gle.com/file/d/13dBvbCTMVmko67B7GZGH7ck_HwIVmJ_2-rT7MbU_dqQUGQz6YeRpb-rY1ucz/edit?usp=sharing.
- ↑ 7.0 7.1 Schmidt, Carla; Lenz, Christof; Grote, Michael; LüHrmann, Reinhard; Urlaub, Henning (2010). "Determination of Protein Stoichiometry within Protein Complexes Using Absolute Quantification and Multiple Reaction Monitoring". Analytical Chemistry 82 (7): 2784–2796. doi:10.1021/ac902710k. PMID 20225856.
- ↑ Geng, Jiefei; Klionsky, Daniel J. (2010). "Determining Atg protein stoichiometry at the phagophore assembly site by fluorescence microscopy". Autophagy 6 (1): 144–147. doi:10.4161/auto.6.1.10249. PMID 20131413.
- ↑ Das, Somes K.; Darshi, Manjula; Cheley, Stephen; Wallace, Mark I.; Bayley, Hagan (2007). "Membrane Protein Stoichiometry Determined from the Step-Wise Photobleaching of Dye-Labelled Subunits". ChemBioChem 8 (9): 994–999. doi:10.1002/cbic.200600474. PMID 17503420.
- ↑ Giraldo, Ana María Villamil; Castello, Pablo Raúl; Flecha, F. Luis González; Moeller, Jesper V.; Delfino, José María; Rossi, Juan Pablo F.C. (2006). "Stoichiometry of lipid-protein interaction assessed by hydrophobic photolabeling". FEBS Letters 580 (2): 607–612. doi:10.1016/j.febslet.2005.12.078. PMID 16412439.
- ↑ Wohlgemuth, Ingo; Lenz, Christof; Urlaub, Henning (2015). "Studying macromolecular complex stoichiometries by peptide‐based mass spectrometry". Proteomics 15 (5–6): 862–879. doi:10.1002/pmic.201400466. PMID 25546807.
- ↑ Smits, Arne H.; Jansen, Pascal W. T. C.; Poser, Ina; Hyman, Anthony A.; Vermeulen, Michiel (2013). "Stoichiometry of chromatin-associated protein complexes revealed by label-free quantitative mass spectrometry-based proteomics". Nucleic Acids Research 41 (1): e28. doi:10.1093/nar/gks941. PMID 23066101.
- ↑ Singh, Avtar; Van Slyke, Alexander L.; Sirenko, Maria; Song, Alexander; Kammermeier, Paul J.; Zipfel, Warren R. (2020). "Stoichiometric analysis of protein complexes by cell fusion and single molecule imaging". Scientific Reports 10 (1): 14866. doi:10.1038/s41598-020-71630-6. PMID 32913201.
- ↑ Hochleitner, Elisabeth O.; Kastner, Berthold; Fröhlich, Thomas; Schmidt, Alexander; Lührmann, Reinhard; Arnold, Georg; Lottspeich, Friedrich (2005). "Protein Stoichiometry of a Multiprotein Complex, the Human Spliceosomal U1 Small Nuclear Ribonucleoprotein". Journal of Biological Chemistry 280 (4): 2536–2542. doi:10.1074/jbc.M409587200. PMID 15525645.
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