ArticleJournal of bacteriology2012
Identification of genes involved in the acetamidino group modification of the flagellin N-linked glycan of Methanococcus maripaludis.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- The Oligosaccharyltransferase AglB Supports Surface-Associated Growth and Iron Oxidation in Methanococcus maripaludis.Applied and environmental microbiology · 2021Article
- A comprehensive history of motility and Archaellation in Archaea.FEMS microbes · 2021Article
- Article
- Identification and characterization of the 4-epimerase AglW from the archaeon Methanococcus maripaludis.Glycoconjugate journal · 2018Article
- Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- Flashy flagella: flagellin modification is relatively common and highly versatile among the Enterobacteriaceae.BMC genomics · 2016Article
- Evidence that biosynthesis of the second and third sugars of the archaellin Tetrasaccharide in the archaeon Methanococcus maripaludis occurs by the same pathway used by Pseudomonas aeruginosa to make a di-N-acetylated sugar.Journal of bacteriology · 2015Article
- Pilin Processing Follows a Different Temporal Route than That of Archaellins in Methanococcus maripaludis.Life (Basel, Switzerland) · 2015Article
- Effects of N-glycosylation site removal in archaellins on the assembly and function of archaella in Methanococcus maripaludis.PloS one · 2015Article
- The archaellum: how Archaea swim.Frontiers in microbiology · 2015Article
- Article
- N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.Microbiology and molecular biology reviews : MMBR · 2014Review
- Article
- Identification of genes involved in the biosynthesis of the third and fourth sugars of the Methanococcus maripaludis archaellin N-linked tetrasaccharide.Journal of bacteriology · 2013Article
- Post-translation modification in Archaea: lessons from Haloferax volcanii and other haloarchaea.FEMS microbiology reviews · 2013Review
- Extreme sweetness: protein glycosylation in archaea.Nature reviews. Microbiology · 2013Review
- Surface appendages of archaea: structure, function, genetics and assembly.Life (Basel, Switzerland) · 2013Review
- Bacterial cell-envelope glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2013Review
- N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.Journal of bacteriology · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-linked glycosylation of protein is a posttranslational modification found in all three domains of life. The flagellin proteins of the archaeon Methanococcus maripaludis are known to be modified with an N-linked tetrasaccharide consisting of N-acetylgalactosamine (GalNAc), a diacetylated glucuronic acid (GlcNAc3NAc), an acetylated and acetamidino-modified mannuronic acid with a substituted threonine group (ManNAc3NAmA6Thr), and a novel terminal sugar residue [(5S)-2-acetamido-2,4-dideoxy-5-O-methyl-α-L-erythro-hexos-5-ulo-1,5-pyranose]. To identify genes involved in biosynthesis of the component sugars of this glycan, three genes, mmp1081, mmp1082, and mmp1083, were targeted for in-frame deletion, based on their annotation and proximity to glycosyltransferase genes known to be involved in assembly of the glycan. Mutants carrying a deletion in any of these three genes remained flagellated and motile. A strain with a deletion of mmp1081 had lower-molecular-mass flagellins in Western blots. Mass spectrometry of purified flagella revealed a truncated glycan with the terminal sugar absent and the threonine residue and the acetamidino group missing from the third sugar. No glycan modification was seen in either the Δmmp1082 or Δmmp1083 mutant grown in complex Balch III medium. However, a glycan identical to the Δmmp1081 glycan was observed when the Δmmp1082 or Δmmp1083 mutant was grown under ammonia-limited conditions. We hypothesize that MMP1082 generates ammonia and tunnels it through MMP1083 to MMP1081, which acts as the amidotransferase, modifying the third sugar residue of the M. maripaludis glycan with the acetamidino group.
Indexed as
Identifiers
What OpenQuestion holds
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.