Effect of Nε-acetylation on the Enzymatic Activity of Escherichia coli Glyceraldehyde-3-phosphate Dehydrogenase

封面

如何引用文章

全文:

开放存取 开放存取
受限制的访问 ##reader.subscriptionAccessGranted##
受限制的访问 订阅存取

详细

The regulation of cellular metabolism is a topic of interest for both fundamental and applied science, as the findings can be used in various biotechnological industries. One of the universal regulatory mechanisms that affects most cellular processes is the acetylation of lysine residues in central metabolic enzymes, such as glyceraldehyde-3-phosphate dehydrogenase. In this work, we investigated the effect of acetylation and deacetylation on the activity of both wild type and mutant E. coli glyceraldehyde-3-phosphate dehydrogenase. We found that in vitro acetylation of wild-type GAPDH by PatZ acetyltransferase increased its enzymatic activity by twofold, while subsequent deacetylation restored the activity to initial level. For mutant forms of glyceraldehyde-3-phosphate dehydrogenase, we demonstrated that the introduction of additional acetylation sites due to mutations altered the impact of acetylation/deacetylation processes on glyceraldehyde-3-phosphate dehydrogenase activity. Our data suggest a re-evaluation of the role of acetylation in regulating glyceraldehyde-3-phosphate dehydrogenase activity and its involvement in E. coli metabolism.

作者简介

N. Plekhanova

Federal Research Centre «Fundamentals of Biotechnology of the Russian Academy of Sciences

编辑信件的主要联系方式.
Email: plekhanovans@mail.ru
Russia, 119071, Moscow

I. Altman

MIREA – Russian Technological University

Email: plekhanovans@mail.ru
Russia, 119454, Moscow

M. Yurkova

Federal Research Centre «Fundamentals of Biotechnology of the Russian Academy of Sciences

Email: plekhanovans@mail.ru
Russia, 119071, Moscow

A. Fedorov

Federal Research Centre «Fundamentals of Biotechnology of the Russian Academy of Sciences

Email: plekhanovans@mail.ru
Russia, 119071, Moscow

参考

  1. Kuhn M.L., Zemaitaitis B., Hu L.I., Sahu A., Sorensen D., Minasov G. et al. //PLoS ONE. 2014. V. 9. № 4. P. e94816. https://doi.org/10.1371/journal.pone.0094816
  2. Wang Q., Zhang Y., Yang C., Xiong H., Lin Y., Yao J. et al. // Science. 2010. V. 327. P. 1004–1007.
  3. Verdin E., Ott M. //Molecular Cell. 2013. T. 51. № 2. C. 132–134.
  4. Slivinskaya E.A., Plekhanova N.S., Altman I.B., Yampolskaya T.A. // Microorganisms. 2022. V. 10. P. 976.https://doi.org/10.3390/microorganisms10050976
  5. Schilling B., Basisty N., Christensen D.G., Sorensen D., Orr J.S., Wolfe A.J. et al. //J. Bacteriol. 2019. V. 201. № 9. https://doi.org/10.1128/JB.00768-18
  6. Castaño-Cerezo S., Bernal V., Post H., Fuhrer T., Cappadona S., Sánchez-Díaz N.C. et al. //Molecular Systems Biology. 2014. V. 10. P. 762. https://doi.org/10.15252/msb.20145227
  7. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual. 2nd. ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press, 1989. 1625 p.
  8. Thomason L.C., Costantino N., Court D.L. //CP Molecular Biology. 2007. V. 79. https://doi.org/10.1002/0471142727.mb0117s79
  9. Datsenko K.A., Wanner B.L. //Proc. Natl. Acad. Sci. USA. 2000. V. 97. P. 6640–6645.
  10. Lamed R., Zeikus J.G. // J Bacteriol. 1980. V. 141. P. 1251–1257.
  11. Laemmli U.K. //Nature. 1970. V. 227. P. 680–685.
  12. Song L., Wang G., Malhotra A., Deutscher M.P., Liang W. // Nucleic Acids Res. 2016. V. 44. P. 1979–1988.
  13. Wittig I., Karas M., Schägger H. // Molecular & Cellular Proteomics. 2007. V. 6. P. 1215–1225.
  14. Zhou X., Zheng W., Li Y., Pearce R., Zhang C., Bell E.W. et al. // Nat Protoc. 2022. V. 17. № 10. P. 2326–2353.
  15. Brooks B.R., Bruccoleri R.E., Olafson B.D., States D.J., Swaminathan S., Karplus M. // J. Comput. Chem. 1983. V. 4. P. 187–217.
  16. Bikadi Z., Hazai E. // J. Cheminform. 2009. V. 1. P. 15. https://doi.org/10.1186/1758-2946-1-15
  17. Halgren T.A. // Encyclopedia of Computational Chemistry. UK: John Wiley & Sons, 2002. https://doi.org/10.1002/0470845015.cma012m
  18. Xia L., Kong X., Song H., Han Q., Zhang S. // Plant Communications. 2022. V. 3. P. 100266. https://doi.org/10.1016/j.xplc.2021.100266
  19. Okanishi H., Kim K., Masui R., Kuramitsu S. // J. Proteome Res. 2013. V. 12. P. 3952–3968.
  20. Smith K., Shen F., Lee H.J., Chandrasekaran S. // iScience. 2022. V. 25. P. 103730. https://doi.org/10.1016/j.isci.2021.103730
  21. Ketema E.B., Lopaschuk G.D. // Front. Cardiovasc. Med. 2021. V. 8. P. 723996. https://doi.org/10.3389/fcvm.2021.723996
  22. Li T., Liu M., Feng X., Wang Z., Das I., Xu Y. et al. // J. Biol. Chem. 2014. V. 289. P. 3775–3785.
  23. Ventura M., Mateo F., Serratosa J., Salaet I., Carujo S., Bachs O. et al. // Int. J. Biochem. Cell Biol. 2010. V. 42. P. 1672–1680.
  24. Zhang H., Zhao Y., Zhou D.X. // Nucleic Acids Research. 2017. V. 45. P. 12241–12255.
  25. Baba T., Ara T., Hasegawa M., Takai Y., Okumura Y., Baba M., Datsenko K.A. et al. // Molecular Systems Biology. 2006. V. 2. P. 2006. https://doi.org/10.1038/msb4100050
  26. Crooks G.E., Hon G., Chandonia J.-M., Brenner S.E. // Genome Res. 2004. V. 14. P. 1188–1190.

补充文件

附件文件
动作
1. JATS XML
下载
2.

下载 (101KB)
索引源数据
3.

下载 (685KB)
索引源数据
4.

下载 (445KB)
索引源数据

版权所有 © Н.С. Плеханова, И.Б. Альтман, М.С. Юркова, А.Н. Федоров, 2023