FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1601498895> ?p ?o ?g. }

• W1601498895 endingPage "104" @default.
• W1601498895 startingPage "25" @default.
• W1601498895 abstract "Methylation of cytosines and adenines in DNA is a widespread epigenetic mark in both prokaryotes and eukaryotes. In eukaryotes, it has a profound influence on chromatin structure and dynamics. Recent advances in genomics and biochemistry have considerably elucidated the functions and provenance of these DNA modifications. DNA methylases appear to have emerged first in bacterial restriction–modification (R–M) systems from ancient RNA-modifying enzymes, in transitions that involved acquisition of novel catalytic residues and DNA-recognition features. DNA adenine methylases appear to have been acquired by ciliates, heterolobosean amoeboflagellates, and certain chlorophyte algae. Six distinct clades of cytosine methylases, including the DNMT1, DNMT2, and DNMT3 clades, were acquired by eukaryotes through independent lateral transfer of their precursors from bacteria or bacteriophages. In addition to these, multiple adenine and cytosine methylases were acquired by several families of eukaryotic transposons. In eukaryotes, the DNA-methylase module was often combined with distinct modified and unmodified peptide recognition domains and other modules mediating specialized interactions, for example, the RFD module of DNMT1 which contains a permuted Sm domain linked to a helix-turn-helix domain. In eukaryotes, the evolution of DNA methylases appears to have proceeded in parallel to the elaboration of histone-modifying enzymes and the RNAi system, with functions related to counter-viral and counter-transposon defense, and regulation of DNA repair and differential gene expression being their primary ancestral functions. Diverse DNA demethylation systems that utilize base-excision repair via DNA glycosylases and cytosine deaminases appear to have emerged in multiple eukaryotic lineages. Comparative genomics suggests that the link between cytosine methylation and DNA glycosylases probably emerged first in a novel R–M system in bacteria. Recent studies suggest that the 5mC is not a terminal DNA modification, with enzymes of the Tet/JBP family of 2-oxoglutarate- and iron-dependent dioxygenases further hydroxylating it to form 5-hydroxymethylcytosine (5hmC). These enzymes emerged first in bacteriophages and appear to have been transferred to eukaryotes on one or more occasions. Eukaryotes appear to have recruited three major types of DNA-binding domains (SRA/SAD, TAM/MBD, and CXXC) in discriminating DNA with methylated or unmethylated cytosines. Analysis of the domain architectures of these domains and the DNA methylases suggests that early in eukaryotic evolution they developed a close functional link with SET-domain methylases and Jumonji-related demethylases that operate on peptides in chromatin proteins. In several eukaryotes, other functional connections were elaborated in the form of various combinations between domains related to DNA methylation and those involved in ATP-dependent chromatin remodeling and RNAi. In certain eukaryotes, such as mammals and angiosperms, novel dependencies on the DNA methylation system emerged, which resulted in it affecting unexpected aspects of the biology of these organisms such as parent–offspring interactions. In genomic terms, this was reflected in the emergence of new proteins related to methylation, such as Stella. The well-developed methylation systems of certain heteroloboseans, stramenopiles, chlorophytes, and haptophyte indicate that these might be new model systems to explore the relevance of DNA modifications in eukaryotes." @default.
• W1601498895 created "2016-06-24" @default.
• W1601498895 creator A5026460419 @default.
• W1601498895 creator A5026932356 @default.
• W1601498895 creator A5045663522 @default.
• W1601498895 date "2011-01-01" @default.
• W1601498895 modified "2023-10-03" @default.
• W1601498895 title "Natural History of Eukaryotic DNA Methylation Systems" @default.
• W1601498895 cites W1490231232 @default.
• W1601498895 cites W1493102094 @default.
• W1601498895 cites W1500702901 @default.
• W1601498895 cites W1544893850 @default.
• W1601498895 cites W1569208976 @default.
• W1601498895 cites W1592521963 @default.
• W1601498895 cites W1597833756 @default.
• W1601498895 cites W1605104953 @default.
• W1601498895 cites W1625510017 @default.
• W1601498895 cites W1637312052 @default.
• W1601498895 cites W1659768997 @default.
• W1601498895 cites W1715660697 @default.
• W1601498895 cites W1723187838 @default.
• W1601498895 cites W1802567635 @default.
• W1601498895 cites W1838266191 @default.
• W1601498895 cites W1839035480 @default.
• W1601498895 cites W1845321470 @default.
• W1601498895 cites W1857890191 @default.
• W1601498895 cites W1867958153 @default.
• W1601498895 cites W1916132949 @default.
• W1601498895 cites W1959952659 @default.
• W1601498895 cites W1964797108 @default.
• W1601498895 cites W1965428844 @default.
• W1601498895 cites W1965902487 @default.
• W1601498895 cites W1966452733 @default.
• W1601498895 cites W1968466047 @default.
• W1601498895 cites W1969331541 @default.
• W1601498895 cites W1969900557 @default.
• W1601498895 cites W1970107572 @default.
• W1601498895 cites W1970608287 @default.
• W1601498895 cites W1971978509 @default.
• W1601498895 cites W1974333880 @default.
• W1601498895 cites W1975954127 @default.
• W1601498895 cites W1976778637 @default.
• W1601498895 cites W1977063334 @default.
• W1601498895 cites W1978082739 @default.
• W1601498895 cites W1978192207 @default.
• W1601498895 cites W1979431956 @default.
• W1601498895 cites W1979733539 @default.
• W1601498895 cites W1980643159 @default.
• W1601498895 cites W1981463058 @default.
• W1601498895 cites W1981509506 @default.
• W1601498895 cites W1981534594 @default.
• W1601498895 cites W1981888730 @default.
• W1601498895 cites W1982138913 @default.
• W1601498895 cites W1984451904 @default.
• W1601498895 cites W1984576980 @default.
• W1601498895 cites W1986167448 @default.
• W1601498895 cites W1986567024 @default.
• W1601498895 cites W1987189614 @default.
• W1601498895 cites W1989185112 @default.
• W1601498895 cites W1989793645 @default.
• W1601498895 cites W1990125225 @default.
• W1601498895 cites W1990654003 @default.
• W1601498895 cites W1992004457 @default.
• W1601498895 cites W1992048312 @default.
• W1601498895 cites W1992159506 @default.
• W1601498895 cites W1992264141 @default.
• W1601498895 cites W1993278112 @default.
• W1601498895 cites W1994586595 @default.
• W1601498895 cites W1994926048 @default.
• W1601498895 cites W1995265002 @default.
• W1601498895 cites W1997974036 @default.
• W1601498895 cites W1998270389 @default.
• W1601498895 cites W2000549627 @default.
• W1601498895 cites W2001373252 @default.
• W1601498895 cites W2001476164 @default.
• W1601498895 cites W2001728345 @default.
• W1601498895 cites W2002944556 @default.
• W1601498895 cites W2003258770 @default.
• W1601498895 cites W2003788507 @default.
• W1601498895 cites W2005311687 @default.
• W1601498895 cites W2005458309 @default.
• W1601498895 cites W2005643112 @default.
• W1601498895 cites W2006346753 @default.
• W1601498895 cites W2006377201 @default.
• W1601498895 cites W2007905902 @default.
• W1601498895 cites W2009070980 @default.
• W1601498895 cites W2011700794 @default.
• W1601498895 cites W2013562830 @default.
• W1601498895 cites W2015468898 @default.
• W1601498895 cites W2017414701 @default.
• W1601498895 cites W2018304597 @default.
• W1601498895 cites W2018512856 @default.
• W1601498895 cites W2019683899 @default.
• W1601498895 cites W2020702702 @default.
• W1601498895 cites W2020767030 @default.
• W1601498895 cites W2020798236 @default.
• W1601498895 cites W2021893136 @default.
• W1601498895 cites W2022405729 @default.

• next