Sandbox Reserved 1644: Difference between revisions

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<p align="justify">Lon proteins are grouped into two families, '''LonA''' and '''LonB'''. The human protein LonP1 is part of the LonA proteins <ref>« The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease | Scientific Reports ». Consulté le 13 janvier 2021. https://www.nature.com/articles/srep33631.
<p align="justify">Lon proteins are grouped into two families, '''LonA''' and '''LonB'''. The human protein LonP1 is part of the LonA proteins <ref>« The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease | Scientific Reports ». Consulté le 13 janvier 2021. https://www.nature.com/articles/srep33631.
</ref>. This protein has three isoforms obtained by [https://en.wikipedia.org/wiki/Alternative_splicing alternative splicing] of the portion of DNA coding for this protein <ref>He, Lihong, Dongyang Luo, Fan Yang, Chunhao Li, Xuegong Zhang, Haiteng Deng, et Jing-Ren Zhang. « Multiple domains of bacterial and human Lon proteases define substrate selectivity ». Emerging Microbes & Infections 7 (17 août 2018). https://doi.org/10.1038/s41426-018-0148-4.
</ref>. This protein has three isoforms obtained by [https://en.wikipedia.org/wiki/Alternative_splicing alternative splicing] of the portion of DNA coding for this protein <ref>He, Lihong, Dongyang Luo, Fan Yang, Chunhao Li, Xuegong Zhang, Haiteng Deng, et Jing-Ren Zhang. « Multiple domains of bacterial and human Lon proteases define substrate selectivity ». Emerging Microbes & Infections 7 (17 août 2018). https://doi.org/10.1038/s41426-018-0148-4.
</ref>. here is a possible cleavage at the amino and carboxyl ends ; thus, there is an isoform for each possible site of cleavage and one for both. <ref>Pomatto, L. C., Carney, C., Shen, B., Wong, S., Halaszynski, K., Salomon, M. P., ... & Tower, J. (2017). The mitochondrial Lon protease is required for age-specific and sex-specific adaptation to oxidative stress. Current Biology, 27(1), 1-15.</ref>
</ref>: here is a possible cleavage at the amino and carboxyl ends ; thus, there is an isoform for each possible site of cleavage and one for both. <ref>Pomatto, L. C., Carney, C., Shen, B., Wong, S., Halaszynski, K., Salomon, M. P., ... & Tower, J. (2017). The mitochondrial Lon protease is required for age-specific and sex-specific adaptation to oxidative stress. Current Biology, 27(1), 1-15.</ref>
Globally there is a great diversity of Lon proteins, but they are all organized in an oligomeric ring structure, mostly hexameric structure with identical subunits.
Globally there is a great diversity of Lon proteins, but they are all organized in an oligomeric ring structure, mostly hexameric structure with identical subunits.
Lon proteins are therefore an hexameric chambered [https://en.wikipedia.org/wiki/Protease protease] complex. (This structure is similar to yeast [https://www.yeastgenome.org/locus/S000000118 Pim1] )
Lon proteins are therefore an hexameric chambered [https://en.wikipedia.org/wiki/Protease protease] complex. (This structure is similar to yeast [https://www.yeastgenome.org/locus/S000000118 Pim1] )