Browsing by Subject "Methanococcus maripaludis"
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Item Data for S-layer glycosylation supports surface-associated growth and iron oxidation in Methanococcus maripaludis(2021-02-05) Holten, Matthew P; Fonseca, Dallas R; Costa, Kyle C; kcosta@umn.edu; Costa, Kyle C; Costa LabMost microbial organisms grow as surface-attached communities known as biofilms. However, the mechanisms whereby methanogenic archaea grow attached to surfaces have remained understudied. Here, we show that the oligosaccharyltransferase AglB is essential for growth of Methanococcus maripaludis strain JJ on glass or metal surfaces. AglB glycosylates several cellular structures such as pili, archaella, and the cell surface layer (S-layer). We show that the S-layer of strain JJ, but not strain S2, is a glycoprotein, that only strain JJ was capable of growth on surfaces, and that deletion of aglB blocked S-layer glycosylation and abolished surface-associated growth. A strain JJ mutant lacking structural components of the type IV-like pilus did not have a growth defect under any conditions tested, while a mutant lacking the pre-flagellin peptidase (∆flaK) was only defective for surface growth when formate was provided as the sole electron donor. Finally, for strains that are capable of Fe0 oxidation, we show that deletion of aglB decreases the rate of anaerobic Fe0 oxidation, presumably due to decreased association of biomass with the Fe0 surface. Together, these data provide an initial characterization of surface-associated growth in a member of the methanogenic archaea.Item Transcriptomics analysis (RNA-sequencing) of Methanococcus maripaludis wild-type strain and moeA deletion mutant.(2023-10-02) Abdul Halim, Mohd Farid; Costa, Kyle C.; Fonseca, Dallas; Niehaus, Thomas; kcosta@umn.edu; Costa, Kyle C.; University of Minnesota Costa LabTranscriptomic analysis of total RNA for Methanococcus maripaludis grown in McCas-formate medium. The data compared the RNA abundance between the wild-type strain and the mutant strain with the gene encoding molybdopterin molybdotransferase (moeA, MMP1619) deletion. Released for the submission of manuscript for publication.