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  Ubiquitin found in the archaebacterium Thermoplasma acidophilum

Wolf, S., Lottspeich, F., & Baumeister, W. (1993). Ubiquitin found in the archaebacterium Thermoplasma acidophilum. FEBS Letters., 326(1-3), 42-44.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-73DB-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-73DC-8
Genre: Journal Article

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 Creators:
Wolf, S.1, Author              
Lottspeich, F.1, Author              
Baumeister, W.1, Author              
Affiliations:
1External Organizations, ou_persistent22              

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Free keywords: Amino Acid Sequence; Electrophoresis, Gel, Two-Dimensional; Isoelectric Focusing; Isoelectric Point; Molecular Sequence Data; Molecular Weight; *Thermoplasma/ch [Chemistry]; *Ubiquitins/an [Analysis]; Ubiquitins/ch [Chemistry]
 Abstract: Systematic N-terminal sequencing of the low molecular weight proteins from Thermoplasma acidophilum separated by two-dimensional poly-acrylamide gel electrophoresis led to the discovery of a polypeptide with an apparent M(r) of 4.5 kDa identical as its first 18 amino acid residues to human ubiquitin. The occurrence of ubiquitin and proteasomes in an archaebacterium strongly suggests that ATP-ubiquitin-dependent proteolysis is a cellular function that developed early in evolution.

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 Dates: 1993
 Publication Status: Published in print
 Pages: -
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 Rev. Type: -
 Identifiers: eDoc: 318581
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Title: FEBS Letters.
Source Genre: Journal
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Pages: - Volume / Issue: 326 (1-3) Sequence Number: - Start / End Page: 42 - 44 Identifier: -