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  Bioinformatic analysis of ClpS, a protein module involved in prokaryotic and eukaryotic protein degradation

Lupas, A., & Koretke, K. (2003). Bioinformatic analysis of ClpS, a protein module involved in prokaryotic and eukaryotic protein degradation. Journal of Structural Biology, 141(1), 77-83. doi:10.1016/s1047-8477(02)00582-8.

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 Creators:
Lupas, AN1, Author                 
Koretke, KK, Author
Affiliations:
1Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375791              

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 Abstract: ClpS is a small protein, usually encoded immediately upstream of ClpA in the genomes of proteobacteria. Recent results show that it is a molecular adaptor for substrate recognition by ClpA in Escherichia coli. We analyzed ClpS by bioinformatic methods and found that ClpS homologs are also found in organisms that lack ClpA, such as actinobacteria, cyanobacteria, and plant chloroplasts. Furthermore, ClpS is homologous to a domain in the eukaryotic E3 ubiquitin ligase, N-recognin. This domain has previously been described as responsible for the recognition of type 2 N-end rule substrates. Despite very low levels of sequence similarity to proteins of known structure, there appears to be substantial structural similarity between ClpS and the C-terminal domain of ribosomal protein L7/12 (1CTF).

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 Dates: 2003-01
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: DOI: 10.1016/s1047-8477(02)00582-8
PMID: 12576022
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Title: Journal of Structural Biology
  Abbreviation : J. Struct. Biol.
Source Genre: Journal
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Publ. Info: San Diego, CA : Elsevier
Pages: - Volume / Issue: 141 (1) Sequence Number: - Start / End Page: 77 - 83 Identifier: ISSN: 1047-8477
CoNE: https://pure.mpg.de/cone/journals/resource/954922650160