Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown.
TLDR
Results indicate that the activated amino acid residue of the polypeptide is COOH-terminal glycine.About:
This article is published in Journal of Biological Chemistry.The article was published on 1981-02-25 and is currently open access. It has received 123 citations till now. The article focuses on the topics: Residue (chemistry) & Amino acid.read more
Citations
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Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown.
TL;DR: Observations indicate that the function of E2 is the transfer of activated ubiquitin to the site of conjugation in the form of an E2-ubiquitin thiol ester intermediate, which is consistent with the notion that a covalent linkage is formed between E2 and Sepharose-bound ubiquitIn.
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Proteolysis: from the lysosome to ubiquitin and the proteasome.
TL;DR: In this paper, the ubiquitin-proteasome system resolved the enigma of how cellular proteins are degraded in the lysosome and showed that non-lysosomal pathways have an important role in intracellular proteolysis, although their identity and mechanisms of action remained obscure.
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Muscle Protein Breakdown and the Critical Role of the Ubiquitin-Proteasome Pathway in Normal and Disease States
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The ubiquitin-proteasome system.
TL;DR: The key observations that led to the discovery of ubiquitin-proteasome system (UPS) are recounted and some key roles of the UPS in different areas of biology and the use of inhibitors of this pathway as possible drug targets are discussed.
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Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin–proteasome system and onto human diseases and drug targeting
TL;DR: The discovery of the ubiquitin–proteasome system resolved the enigma and it is recognized that degradation of intracellular proteins is involved in regulation of a broad array of cellular processes, such as cell cycle and division, regulation of transcription factors and assurance of the cellular quality control.
References
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Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis.
TL;DR: A sequence of reactions in which the linkage of APF-1 to the substrates is followed by the proteolytic breakdown of the substrate is proposed to explain the role of ATP.
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A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes.
TL;DR: In this paper, the degradation of denatured globin in reticulocyte lysates is markedly stimulated by ATP, and the system is now resolved into two components, designated fractions I and II, in the order of their elution from DEAE-cellulose.
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ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation.
TL;DR: The heat-stable polypeptide (APF-1) required for ATP-dependent proteolysis in reticulocytes enters into high molecular weight conjugates upon incubation with the fraction of reticULocytes that is retained by DEAE-cellulose, suggesting that the conjugate formation requires ATP and Mg2+ and its inhibited by N-ethylmaleimide.
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Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes.
TL;DR: Evidence is provided that APF-1 is ubiquitin, a highly conserved heat-stable polypeptide found universally in nature, and a similar role in degradation and proteolytic processing in other cells is likely.
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The complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cells.
TL;DR: The complete amino acid sequence was determined for bovine ubiquitin, and adenylate cyclase stimulating polypeptide, which is probably represented universally in living cells and supported by amino acid and parital sequence anlysis of fragments obtained by digestion of maleated ubiquit in with chymotrypsin or staphylococcal protease.