ArticleJournal of bacteriology2006
Active-site residues in the type IV prepilin peptidase homologue PibD from the archaeon Sulfolobus solfataricus.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 48 citations in OpenAlex.
- Adhesion pilus retraction powers twitching motility in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius.Nature communications · 2024Article
- High throughput and targeted screens for prepilin peptidase inhibitors do not identify common inhibitors of eukaryotic gamma-secretase.Expert opinion on drug discovery · 2023Article
- Mechanism of assembly of type 4 filaments: everything you always wanted to know (but were afraid to ask).Microbiology (Reading, England) · 2023Review
- A comprehensive history of motility and Archaellation in Archaea.FEMS microbes · 2021Article
- The switch complex ArlCDE connects the chemotaxis system and the archaellum.Molecular microbiology · 2020Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Structure and function of the archaeal response regulator CheY.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Cloning-independent markerless gene editing in Streptococcus sanguinis: novel insights in type IV pilus biology.Nucleic acids research · 2017Article
- Screening of a Haloferax volcanii Transposon Library Reveals Novel Motility and Adhesion Mutants.Life (Basel, Switzerland) · 2016Article
- Membrane Association and Catabolite Repression of the Sulfolobus solfataricus α-Amylase.Microorganisms · 2015Article
- The archaellum: how Archaea swim.Frontiers in microbiology · 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
- Dissection of key determinants of cleavage activity in signal peptidase III (SPaseIII) PibD.Extremophiles : life under extreme conditions · 2014Article
- Surface appendages of archaea: structure, function, genetics and assembly.Life (Basel, Switzerland) · 2013Review
- Structure and function of the adhesive type IV pilus of Sulfolobus acidocaldarius.Environmental microbiology · 2012Article
- The archaeal cell envelope.Nature reviews. Microbiology · 2011Review
- Article
- S-layer glycoproteins and flagellins: reporters of archaeal posttranslational modifications.Archaea (Vancouver, B.C.) · 2010Review
- Shaping the archaeal cell envelope.Archaea (Vancouver, B.C.) · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Archaeal preflagellin peptidases and bacterial type IV prepilin peptidases belong to a family of aspartic acid proteases that cleave the leader peptides of precursor proteins with type IV prepilin signal sequences. The substrate repertoire of PibD from the crenarchaeon Sulfolobus solfataricus is unusually diverse. In addition to flagellin, PibD cleaves three sugar-binding proteins unique to this species and a number of proteins with unknown function. Here we demonstrate that PibD contains two aspartic acid residues that are essential for cleavage activity. An additional pair of aspartic acids in a large cytoplasmic loop is also important for function and is possibly involved in leader peptide recognition. Combining the results of transmembrane segment predictions and cysteine-labeling experiments, we suggest a membrane topology model for PibD with the active-site aspartic acid residues exposed to the cytosol.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.