Cell Surface Structures of Archaea

Ng, Sandy Y. M.; Zolghadr, Behnam; Driessen, Arnold J. M.; Albers, Sonja‐Verena; Jarrell, Ken F.

doi:10.1128/jb.00546-08

Cited by 61 publications

(39 citation statements)

References 94 publications

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“…The wider than expected utilization of type IV pilin-like signal sequences, as well as the lower enzyme stringency, is most probably a specialization that the PibD enzyme has undergone (4). These additional sugar-binding substrates have been hypothesized to assemble into a pilus-like "bindosome" on the surface of the cell (3,24).…”

Section: Discussionmentioning

confidence: 99%

Different Minimal Signal Peptide Lengths Recognized by the Archaeal Prepilin-Like Peptidases FlaK and PibD

VanDyke

Chaban

et al. 2009

J Bacteriol

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In Archaea, the preflagellin peptidase (a type IV prepilin-like peptidase designated FlaK in Methanococcus voltae and Methanococcus maripaludis) is the enzyme that cleaves the N-terminal signal peptide from preflagellins. In methanogens and several other archaeal species, the typical flagellin signal peptide length is 11 to 12 amino acids, while in other archaea preflagellins possess extremely short signal peptides. A systematic approach to address the signal peptide length requirement for preflagellin processing is presented in this study. M. voltae preflagellin FlaB2 proteins with signal peptides 3 to 12 amino acids in length were generated and used as a substrate in an in vitro assay utilizing M. voltae membranes as an enzyme source. Processing by FlaK was observed in FlaB2 proteins containing signal peptides shortened to 5 amino acids; signal peptides 4 or 3 amino acids in length were unprocessed. In the case of Sulfolobus solfataricus, where the preflagellin peptidase PibD has broader substrate specificity, some predicted substrates have predicted signal peptides as short as 3 amino acids. Interestingly, the shorter signal peptides of the various mutant FlaB2 proteins not processed by FlaK were processed by PibD, suggesting that some archaeal preflagellin peptidases are likely adapted toward cleaving shorter signal peptides. The functional complementation of signal peptidase activity by FlaK and PibD in an M. maripaludis ⌬flaK mutant indicated that processing of preflagellins was detected by complementation with either FlaK or PibD, yet only FlaK-complemented cells were flagellated. This suggested that a block in an assembly step subsequent to signal peptide removal occurred in the PibD complementation.The bacterial type IV prepilin peptidase (TFPP) is a wellcharacterized enzyme belonging to a family of novel aspartic acid proteases (20). It is responsible for the cleavage of Nterminal signal peptides from prepilins and pseudopilins, prior to their incorporation into the type IV pilus structure (22,30,31). The prepilin peptidase is also responsible for the processing of prepilin-like proteins needed for type II secretion (22). In Archaea, the existence of bacterial TFPP-like enzymes has also been reported, and they have been most extensively studied in relation to the assembly of the archaeal flagellum. In the euryarchaeotes Methanococcus maripaludis and Methanococcus voltae, the preflagellin peptidase FlaK was demonstrated to be responsible for cleaving the N-terminal signal peptide from the preflagellin prior to its incorporation into the growing flagellar filament, a step essential to flagellar assembly (6, 7, 26). In Sulfolobus solfataricus, an acidophilic crenarchaeote, the equivalent enzyme, PibD, was also shown to process preflagellins (4). Site-directed mutagenesis of FlaK and PibD demonstrated that both aspartic acid residues that aligned with aspartic acid residues essential for bacterial TFPP activity were also essential in the archaeal enzymes (6, 32), indicating that the two archaeal peptidases...

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Section: Discussionmentioning

confidence: 99%

Different Minimal Signal Peptide Lengths Recognized by the Archaeal Prepilin-Like Peptidases FlaK and PibD

VanDyke

Chaban

et al. 2009

J Bacteriol

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“…The archaellum (archaeal flagellum) is a surface structure that shares many similarities with the bacterial type IV pilus system (57,58). Archaellar proteins are made as preproteins with N-terminal signal peptides that are cleaved by a prepilin peptidase (FlaK) and assembled by the addition of archaellin subunits to the base of the archaellum.…”

Section: Expression Of Archaella and Other Extracellular Appendages Dmentioning

confidence: 99%

Mechanisms Involved in Fe(III) Respiration by the Hyperthermophilic Archaeon Ferroglobus placidus

Smith

Aklujkar

Risso

et al. 2015

Appl Environ Microbiol

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The hyperthermophilic archaeon Ferroglobus placidus can utilize a wide variety of electron donors, including hydrocarbons and aromatic compounds, with Fe(III) serving as an electron acceptor. In Fe(III)-reducing bacteria that have been studied to date, this process is mediated by c-type cytochromes and type IV pili. However, there currently is little information available about how this process is accomplished in archaea. In silico analysis of the F. placidus genome revealed the presence of 30 genes coding for putative c-type cytochrome proteins (more than any other archaeon that has been sequenced to date), five of which contained 10 or more heme-binding motifs. When cell extracts were analyzed by SDS-PAGE followed by heme staining, multiple bands corresponding to c-type cytochromes were detected. Different protein expression patterns were observed in F. placidus cells grown on soluble and insoluble iron forms. In order to explore this result further, transcriptomic studies were performed. Eight genes corresponding to multiheme c-type cytochromes were upregulated when F. placidus was grown with insoluble Fe(III) oxide compared to soluble Fe(III) citrate as an electron acceptor. Numerous archaella (archaeal flagella) also were observed on Fe(III)-grown cells, and genes coding for two type IV pilin-like domain proteins were differentially expressed in Fe(III) oxidegrown cells. This study provides insight into the mechanisms for dissimilatory Fe(III) respiration by hyperthermophilic archaea.

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“…Archaea have been shown to possess a variety of unusual surface structures, some of which appear to have no bacterial counterpart (3,47). Furthermore, there is evidence from studies of numerous archaea showing that many diverse surface structures are composed of proteins made with type IV pilin-like signal peptides and processed by a type IV prepilin peptidase homologue.…”

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confidence: 99%

“…Furthermore, there is evidence from studies of numerous archaea showing that many diverse surface structures are composed of proteins made with type IV pilin-like signal peptides and processed by a type IV prepilin peptidase homologue. Thus far, flagella, certain pili, Iho670 fibers, and the proposed bindosome all share this feature (3,46,47).…”

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confidence: 99%

Genetic and Mass Spectrometry Analyses of the Unusual Type IV-Like Pili of the ArchaeonMethanococcus maripaludis

Nair

et al. 2011

J Bacteriol

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The structure of pili from the archaeon Methanococcus maripaludis is unlike that of any bacterial pili. However, genetic analysis of the genes involved in the formation of these pili has been lacking until this study. Pili were isolated from a nonflagellated (⌬flaK) mutant and shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to consist primarily of subunits with an apparent molecular mass of 17 kDa. In-frame deletions were created in three genes, MMP0233, MMP0236, and MMP0237, which encode proteins with bacterial type IV pilin-like signal peptides previously identified by in silico methodology as likely candidates for pilus structural proteins. Deletion of MMP0236 or MMP0237 resulted in mutant cells completely devoid of pili on the cell surface, while deletion of the third pilin-like gene, MMP0233, resulted in cells greatly reduced in the number of pili on the surface. Complementation with the deleted gene in each case returned the cells to a piliated state. Surprisingly, mass spectrometry analysis of purified pili identified the major structural pilin as another type IV pilin-like protein, MMP1685, whose gene is located outside the first pilus locus. This protein was found to be glycosylated with an N-linked branched pentasaccharide glycan. Deletion and complementation analysis confirmed that MMP1685 is required for piliation.

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Cell Surface Structures of Archaea

Cited by 61 publications

References 94 publications

Different Minimal Signal Peptide Lengths Recognized by the Archaeal Prepilin-Like Peptidases FlaK and PibD

Different Minimal Signal Peptide Lengths Recognized by the Archaeal Prepilin-Like Peptidases FlaK and PibD

Mechanisms Involved in Fe(III) Respiration by the Hyperthermophilic Archaeon Ferroglobus placidus

Genetic and Mass Spectrometry Analyses of the Unusual Type IV-Like Pili of the ArchaeonMethanococcus maripaludis

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