ArticleExtremophiles : life under extreme conditions2014
Dissection of key determinants of cleavage activity in signal peptidase III (SPaseIII) PibD.
Article in Extremophiles : life under extreme conditions, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 16 citations in OpenAlex.
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- Electron cryo-microscopy reveals the structure of the archaeal thread filament.Nature communications · 2022Article
- A comprehensive history of motility and Archaellation in Archaea.FEMS microbes · 2021Article
- Pilin Processing Follows a Different Temporal Route than That of Archaellins in Methanococcus maripaludis.Life (Basel, Switzerland) · 2015Article
- Archaeal type IV pili and their involvement in biofilm formation.Frontiers in microbiology · 2015Article
- Archaeal membrane-associated proteases: insights on Haloferax volcanii and other haloarchaea.Frontiers in microbiology · 2015Review
- The archaellum: how Archaea swim.Frontiers in microbiology · 2015Article
- International conference on extremophiles 2014.Extremophiles : life under extreme conditions · 2014Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Archaea, type IV prepilins and prearchaellins are processed by designated signal peptidase III (SPaseIII) prior to their incorporation into pili and the archaellum, respectively. These peptidases belong to the family of integral membrane aspartic acid proteases that contain two essential aspartate residues of which the second aspartate is located in a conserved GxGD motif. To this group also bacterial type IV prepilin peptidases, Alzheimer disease-related secretases, signal peptide peptidases and signal peptide peptidase-like proteases in humans belong. Here we have performed detailed in vivo analyses to understand the cleavage activity of PibD, SPaseIII from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. Using an already established in vivo heterologous system cleavage assay, we could successfully identify the key amino acid residues essential for catalysis of PibD. Furthermore, in trans complementation of a pibD S. acidocaldarius deletion mutant with PibD variants having substituted key amino acids has consolidated our observations of the importance of these residues in catalysis. Based on our data, we propose to re-define class III peptidases/type IV prepilin/prearchaellin peptidases as GxHyD group (rather than GxGD) of proteases [Hy-hydrophobic amino acid].
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