Characterizing the DNA Methyltransferases of Haloferax volcanii via Bioinformatics, Gene Deletion, and SMRT Sequencing

Genes
Matthew OuelletteR Thane Papke

Abstract

DNA methyltransferases (MTases), which catalyze the methylation of adenine and cytosine bases in DNA, can occur in bacteria and archaea alongside cognate restriction endonucleases (REases) in restriction-modification (RM) systems or independently as orphan MTases. Although DNA methylation and MTases have been well-characterized in bacteria, research into archaeal MTases has been limited. A previous study examined the genomic DNA methylation patterns (methylome) of the halophilic archaeonHaloferax volcanii, a model archaeal system which can be easily manipulated in laboratory settings, via single-molecule real-time (SMRT) sequencing and deletion of a putative MTase gene (HVO_A0006). In this follow-up study, we deleted other putative MTase genes inH. volcaniiand sequenced the methylomes of the resulting deletion mutants via SMRT sequencing to characterize the genes responsible for DNA methylation. The results indicate that deletion of putative RM genesHVO_0794,HVO_A0006, andHVO_A0237in a single strain abolished methylation of the sole cytosine motif in the genome (Cm4TAG). Amino acid alignments demonstrated thatHVO_0794shares homology with characterized cytosine CTAG MTases in other organisms, indicating that this MTase is respon...Continue Reading

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Citations

Jul 5, 2019·Microbiology Resource Announcements·Shiladitya DasSarmaRichard J Roberts
Apr 12, 2020·Genes·Mike Dyall-SmithFriedhelm Pfeiffer
Dec 2, 2020·Open Biology·Patricia Pérez-ArnaizThorsten Allers
May 15, 2019·Journal of Molecular Biology·Travis J SandersThomas J Santangelo

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Datasets Mentioned

BETA
CAA48447
ADQ20483
AAB98988
CAP14114
SSF53335
AAS39772
ABS55549
AAM24756
AAG18733
AAC77304

Methods Mentioned

BETA
Restriction Modification
PCR
electrophoresis
gene knock-in

Software Mentioned

PSI
PhyML
RS
_ Modification _ and _ Motif _ Analysis .
BLAST
blastp )
blastp
SMRT Portal
muscle
Clustal X2

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