Ubiquitin Structure & Function: Difference between revisions
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=Introduction= | =Introduction= | ||
Ubiquitin is one of the most highly conserved eukaryotic proteins. Primary structures found throughout ubiquitin are identical in all bovine, insects and human ubiquitin <ref name="mainpaper"/>. The only difference observed amongst these species is seen in the terminal Gly-Gly residues. Yeast and oat ubiquitin only differ in three of the 76 residues when compared to ubiquitin found in higher eukaryotes<ref name="mainpaper"/>. | Ubiquitin is one of the most highly conserved eukaryotic proteins. Primary structures found throughout ubiquitin are identical in all bovine, insects and human ubiquitin <ref name="mainpaper"/>. The only difference observed amongst these species is seen in the terminal Gly-Gly residues. Yeast and oat ubiquitin only differ in three of the 76 residues when compared to ubiquitin found in higher eukaryotes<ref name="mainpaper"/>. | ||
[[image:1ubiq.png| thumb |none | upright=2.0 |Ubiquitin structure: Arg74 in pink and Gly75 Gly76 in white.]] | |||
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[http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ubq ConSurf]. | [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ubq ConSurf]. | ||
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Ubiquitin can not only be found in the nucleus, but in the cytoplasm and cell-surface membrane as well<ref name="mainpaper"/>. | Ubiquitin can not only be found in the nucleus, but in the cytoplasm and cell-surface membrane as well<ref name="mainpaper"/>. | ||
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Infectious agents can manipulate ubiquitin or deubiquitination and one such protein is Chlamydia trachomatis. Chlamydia trachomatis' protein Cdu-1 catalyzes the hydrolysis of ubiquitin chains from Mcl-1. When polyubiquitnated, Mcl-1 is destined to be degraded by the proteasome, lowering the level of Mcl-1 and subsequently leading to apoptosis. The activity of Cdu-1 counteracts this by removing the ubiquitin, thus leading to higher levels of Mcl-1 in the cell. Additional information can be found here [[User:Karsten Theis/5B5Q]] | Infectious agents can manipulate ubiquitin or deubiquitination and one such protein is Chlamydia trachomatis. Chlamydia trachomatis' protein Cdu-1 catalyzes the hydrolysis of ubiquitin chains from Mcl-1. When polyubiquitnated, Mcl-1 is destined to be degraded by the proteasome, lowering the level of Mcl-1 and subsequently leading to apoptosis. The activity of Cdu-1 counteracts this by removing the ubiquitin, thus leading to higher levels of Mcl-1 in the cell. Additional information can be found here [[User:Karsten Theis/5B5Q]] | ||
SEE ALSO [[Tumor susceptibility gene 101]] | |||
</StructureSection> | </StructureSection> | ||
