Literature DB >> 2335242

The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated.

F Tokunaga1, R Aruga, S Iwanaga, K Tanaka, A Ichihara, T Takao, Y Shimonishi.   

Abstract

Rat liver proteasome (multicatalytic proteinase complex) is a 20S-ring shaped particle having a molecular mass of 750 kDa, and is composed of at least 13 non-identical components ranging from 21 to 31 kDa in size. We found here that the NH2-terminal residues of all the known 13 components, except for C5, are not reactive to phenylisothiocyanate. Among them, components C2, C3 and C8 are blocked in their NH2-termini with N alpha-acetyl-Met, N alpha-acetyl-Ala, and N alpha-acetyl-Ser, respectively. The NH2-terminal portions of C2, C3, and C8 exhibit sequence similarity to one another, but that of the non-blocked component C5 differs from those of C2, C3, and C8.

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Year:  1990        PMID： 2335242     DOI： 10.1016/0014-5793(90)81417-m

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  9 in total

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Authors:  R Medina; S S Wing; A L Goldberg
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Authors:  Max J Dörfel; Gholson J Lyon
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5.  Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes.

Authors:  W E Mitch; R Medina; S Grieber; R C May; B K England; S R Price; J L Bailey; A L Goldberg
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7.  The N-terminal penultimate residue of 20S proteasome alpha1 influences its N(alpha) acetylation and protein levels as well as growth rate and stress responses of Haloferax volcanii.

Authors:  Matthew A Humbard; Guangyin Zhou; Julie A Maupin-Furlow
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8.  Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag.

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Review 9.  Proteasome and Organs Ischemia-Reperfusion Injury.

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  9 in total

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