Ubiquitin and polyubiquitination
15.2 هزار بار بازدید -
11 سال پیش
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This lecture about ubiquitin explains
This lecture about ubiquitin explains the ubiquitination process in protein degradation. http://shomusbiology.weebly.com/
Download the study materials here-
http://shomusbiology.weebly.com/bio-m...
Ubiquitin is a small (8.5 kDa) regulatory protein that has been found in almost all tissues (ubiquitously) of eukaryotic organisms. It was discovered in 1975[1] by Goldstein and further characterized throughout the 1970s and 80s.[2] There are four genes in the human genome that produce ubiquitin; UBB, UBC, UBA52 and RPS27A.[3]
Ubiquitination is a post translational modification (an addition to a protein after it has been made) where ubiquitin is attached to a substrate protein. The addition of ubiquitin can affect proteins in many ways: it can signal for their degradation via the proteasome, alter their cellular location, affect their activity and promote or prevent protein interactions.[4][5][6] Ubiquitination is carried out in three main steps; activation, conjugation and ligation, performed by ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s). The result of this sequential cascade binds ubiquitin to lysine residues on the protein substrate via an isopeptide bond or to the amino group of the protein's N-terminus via a peptide bond.[7][8]
The protein modifications can either be a single ubiquitin protein or chains of ubiquitin. There are different forms of chains, named by which of the seven lysine amino acids are used to link the chain together. Lysine 48-linked chains, linked by the 48th amino acid (a lysine) have been well studied. They are the forms of chains that signal proteins to the proteasome which destroys and recycles proteins.[8] This discovery won the Nobel Prize for chemistry in 2004.[9][10] Lysine 63-linked chains, linked by the 63rd amino acid of ubiquitin (a lysine), regulate processes such as endocytic trafficking, inflammation, translation and DNA repair.[11] Source of the article published in description is Wikipedia. I am sharing their material. Copyright by original content developers.
Link- http://en.wikipedia.org/wiki/Main_Page
Download the study materials here-
http://shomusbiology.weebly.com/bio-m...
Ubiquitin is a small (8.5 kDa) regulatory protein that has been found in almost all tissues (ubiquitously) of eukaryotic organisms. It was discovered in 1975[1] by Goldstein and further characterized throughout the 1970s and 80s.[2] There are four genes in the human genome that produce ubiquitin; UBB, UBC, UBA52 and RPS27A.[3]
Ubiquitination is a post translational modification (an addition to a protein after it has been made) where ubiquitin is attached to a substrate protein. The addition of ubiquitin can affect proteins in many ways: it can signal for their degradation via the proteasome, alter their cellular location, affect their activity and promote or prevent protein interactions.[4][5][6] Ubiquitination is carried out in three main steps; activation, conjugation and ligation, performed by ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s). The result of this sequential cascade binds ubiquitin to lysine residues on the protein substrate via an isopeptide bond or to the amino group of the protein's N-terminus via a peptide bond.[7][8]
The protein modifications can either be a single ubiquitin protein or chains of ubiquitin. There are different forms of chains, named by which of the seven lysine amino acids are used to link the chain together. Lysine 48-linked chains, linked by the 48th amino acid (a lysine) have been well studied. They are the forms of chains that signal proteins to the proteasome which destroys and recycles proteins.[8] This discovery won the Nobel Prize for chemistry in 2004.[9][10] Lysine 63-linked chains, linked by the 63rd amino acid of ubiquitin (a lysine), regulate processes such as endocytic trafficking, inflammation, translation and DNA repair.[11] Source of the article published in description is Wikipedia. I am sharing their material. Copyright by original content developers.
Link- http://en.wikipedia.org/wiki/Main_Page
11 سال پیش
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