N6-Methyladenosine: Difference between revisions

From Wikipedia, the free encyclopedia
Browse history interactively
← Previous editNext edit →
Content deleted Content added
VisualWikitext
updated to include new published findings
added content and context, increased citations and interwiki links.
Line 5: Line 5:
| ImageSize = 150px
| ImageSize = 150px
| IUPACName = ''N''-Methyladenosine
| IUPACName = ''N''-Methyladenosine
| OtherNames = m6A
| OtherNames = m<sup>6</sup>A
| Section1 = {{Chembox Identifiers
| Section1 = {{Chembox Identifiers
| CASNo = 60209-41-8
| CASNo = 60209-41-8
Line 31: Line 31:
}}
}}


'''''N''<sup>6</sup>-Methyladenosine''' ('''m<sup>6</sup>A ''') is an abundant modification in [[mRNA]] and is also found in several [[long non-coding RNA | long non-coding RNAs]], such as [[Xist | ''Xist'']].<ref name=Meyer_etal_2012>{{cite journal|last=Meyer|first=Kate D.|coauthors=Saletore, Yogesh, Zumbo, Paul, Elemento, Olivier, Mason, Christopher E., and Jaffrey, Samie R.|title=Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3′ UTRs and near Stop Codons|journal=Cell|date=17 May 2012|year=2012|doi=10.1016/j.cell.2012.05.003|url=http://www.cell.com/abstract/S0092-8674%2812%2900536-3}}</ref> <ref name="Dominissini2012">{{cite journal|last=Dominissini|first=Dan|coauthors=Moshitch-Moshkovitz, Sharon, Schwartz, Schraga, Salmon-Divon, Mali, Ungar, Lior, Osenberg, Sivan, Cesarkas, Karen, Jacob-Hirsch, Jasmine, Amariglio, Ninette, Kupiec, Martin, Sorek, Rotem, Rechavi, Gideon|title=Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq|journal=Nature|date=29 April 2012|doi=10.1038/nature11112}}</ref> Adenosine methylation is directed by a large m<sup>6</sup>A methyltransferase complex containing [[METTL3]] as the SAM-binding sub-unit. <ref>{{cite journal|last=Bokar|first=JA|coauthors=Shambaugh, ME, Polayes, D, Matera, AG, Rottman, FM|title=Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase|journal=RNA|date=1997 Nov|volume=3|issue=11|pages=1233–47|pmid=9409616|pmc=1369564}}</ref> Mapping of m<sup>6</sup>A in human and mouse RNA has identified over 18,000 m<sup>6</sup>A sites in the transcripts of more than 7,000 human genes with a [[consensus sequence]] of [G/A/U][G>A]m6AC[U>A/C].<ref name=Meyer_etal_2012 /> <ref name=Dominissini2012 /> The localization of individual m<sup>6</sup>A sites in many mRNAs is highly similar between [[human]] and [[mouse]],<ref name=Meyer_etal_2012 /> <ref name=Dominissini2012 /> and transcriptome-wide analysis reveals that m<sup>6</sup>A is found in regions of high evolutionary conservation.<ref name=Meyer_etal_2012 /> m<sup>6</sup>A is found within long internal [[exons]] and is preferentially enriched within 3’ UTRs and around [[stop codons]]. m<sup>6</sup>A within 3’ UTRs is also associated with the presence of microRNA binding sites; roughly 2/3 of the mRNAs which contain an m<sup>6</sup>A site within their 3’ UTR also have at least one microRNA binding site.<ref name=Meyer_etal_2012 />


'''''N''6-Methyladenosine''' (m<sup>6</sup>A ) is an abundant modification in [[mRNA]] and is found within some viruses<ref name=Aloni1>{{cite journal|last=Aloni, Y., Dhar, R., and Khoury, G. |title=Methylation of nuclear simian virus 40 RNAs|journal=J. Virol|year=1979|volume=32|pages=52-60|url=http://www.ncbi.nlm.nih.gov/pmc/articles/PMC353526/}}</ref> <ref name=Bee+K1>{{cite journal|last=Beemon, K., Keith, J.|title=Localization of N6 methyladenosine in Rous sarcoma virus genome|journal=J. Mol. Biol.|year=1977|volume=113|pages=165-179|url=http://www.sciencedirect.com/science/article/pii/002228367790047X}}</ref>, and most eukaryotes including mammals<ref>{{cite journal|last=Desrosiers, R.C., Friderici, K.H., Rottman F.M.|title=Identification of methylated nucleosides in messenger-RNA from Novikoff hepatoma cells|journal=Proc. Natl. Acad Sci|year=1974|volume=71|pages=3971-3975|url=http://www.ncbi.nlm.nih.gov/pmc/articles/PMC434308/}}</ref> <ref>{{cite journal|last=Adams, J.M., and Cory, S.|title=Modified nucleosides and bizarre 5’-terminai in mouse myeloma mRNA|journal=Nature|year=1975|volume=255|pages=28-33|url=http://www.ncbi.nlm.nih.gov/pubmed/1128665}}</ref> <ref name=wei1>{{cite journal|last=Wei, C.M., Gershowitz, A., and Moss B.|title=5’-terminal and internal methylated nucleotide sequences in HeLa cell mRNA|journal=Biochemistry|year=1976|volume=15|pages=397-401|url=http://www.ncbi.nlm.nih.gov/pubmed/174715}}</ref> <ref name=Perry1>{{cite journal|last=Perry, R.P., Kelley, D.E., Fridirici, K., and Rottman, F.M.|title=The methylated constituents of L cell messenger RNA: evidence for an unsual cluster at the 5’-terminus|journal=Cell|year=1975|volume=4|pages=387-394|url=http://www.ncbi.nlm.nih.gov/pubmed/1168101}}</ref>, insects<ref name=Levis1>{{cite journal|last=Levis, R., and Penman, S.|title=5’-Terminal structures of poly(A)+ cytoplasmic messenger-RNA and of poly(A)+ and poly(A)- heterogeneous nuclear-RNA of cells of dipteran Drosophila-melanogaster|journal=J. Mol. Bio|year=1978|volume=120|pages=487-515|url=http://www.sciencedirect.com/science/article/pii/0022283678903509}}</ref>, plants<ref name=Nich1>{{cite journal|last=Nichols, J.L.|title=N6-methyladenosine in maize poly(A)-containing RNA|journal=Plant Science Letters|year=1979|volume=15|pages=357-367|url=http://www.sciencedirect.com/science/article/pii/030442117990141X}}</ref><ref name=Kennedy1>{{cite journal|last=Kennedy, T.D., and Lane, B.G.|title=Wheat embryo ribonucleates. XIII. Methyl-substituted nucleoside constituents and 5’-terminal dinucleotide sequences in bulk poly(A)-rich RNA from imbibing wheat embryos|journal=Can. J. Biochem|year=1979|volume=57|pages=927-931|url=http://www.nrcresearchpress.com/doi/abs/10.1139/o79-112?journalCode=cjbio}}</ref><ref name=Zhong2k8>{{cite journal|last=Zhong, S., Li, H., Bodi, Z., Button, J., Vespa, L., Herzog, M., Fray, R.G|journal=Plant Cell|year=2008|volume=20|pages=1278-1288|url=http://www.plantcell.org/cgi/content/short/tpc.108.058883?keytype=ref&ijkey=tIrXWY7QkOJHRDz}}</ref> and yeast<ref name=Clancy2k2>{{cite journal|last=Clancy, M.J., Shambaugh, M.E., Timpte, C.S., and Bokar, J.A.|title=Induction of sporulation in Saccharomyces cerevisiae leads to the formation of N6-methyladenosine in mRNA: a potential mechanism for the acivity of the IME4 gene|journal=Nucleic Acids Res.|year=2002|volume=30|pages=4509-4518|url=http://www.ncbi.nlm.nih.gov/pubmed/12384598}}</ref> <ref name=Bodi2k10>{{cite journal|last=Bodi, Z., Button, J.D., Grierson, D. and Fray, R.G.|title=Yeast targets for mRNA methylation|journal=Nucleic Acids Research|year=2010|volume=38|pages=5327-5335|url=http://nar.oxfordjournals.org/cgi/content/full/gkq266?ijkey=mhVT4FN3N7Jzjiv&keytype=ref}}</ref>. It and is also found in [[tRNA]], [[rRNA]], and [[small nuclear RNA]] (snRNA) as well as several [[long non-coding RNA]], such as ''[[Xist]]''<ref name=Meyer_etal_2012>{{cite journal|last=Meyer|first=KD.|coauthors=Yogesh S, Zumbo P, Elemento O, Mason CE, Jaffrey SR|title=Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3′ UTRs and near Stop Codons|journal=Cell|year=2012|doi=10.1016/j.cell.2012.05.003|url=http://www.cell.com/abstract/S0092-8674%2812%2900536-3}}</ref> <ref name="Dominissini2012">{{cite journal|last=Dominissini|first=D|coauthors=Moshitch-Moshkovitz S, Schwartz S, Salmon-Divon M, Ungar L, Osenberg S, Cesarkas K, Jacob-Hirsch J, Amariglio N, Kupiec M, Sorek R, Rechavi G|title=Topology of the human and mouse m<sup>6</sup>A RNA methylomes revealed by m<sup>6</sup>A-seq|journal=Nature|Year=2012|doi=10.1038/nature11112}}</ref>.Adenosine methylation is directed by a large m<sup>6</sup>A methyltransferase complex containing METTL3 as the SAM-binding sub-unit <ref>{{cite journal|last=Bokar|first=JA|coauthors=Shambaugh, ME, Polayes, D, Matera, AG, Rottman, FM|title=Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase|journal=RNA|date=1997|volume=3|pages=1233–47|pmid=9409616|pmc=1369564}}</ref> ''In vitro'', this methyltransferase complex preferentially methylates RNA oligonucleotides containing GGACU<ref>{{cite journal|last=Harper, J.E., Miceli, S.M., Roberts R.J., and Manley, J.L.|title=). Sequence specificity of the human messenger-RNA N6-adenosine methylase in vitro|journal=Nucleic Acids Res.|year=1990|volume=18|pages=5735-5741|url=http://www.ncbi.nlm.nih.gov/pmc/articles/PMC332308/}}</ref> and a similar preference was identified ''in vivo'' in mapped m<sup>6</sup>A sites in Rous sarcoma virus genomic RNA<ref name=Kane1>{{cite journal|last=Kane, S.E., and Beemon, K.|title=Precise localization of m<sup>6</sup>A in Rous sarcoma virus RNA reveals clustering of methylation sites: Implications for RNA processing|journal=Mol. Cell. Biol|year=1985|volume=5|pages=2298–2306|url=http://mcb.asm.org/content/5/9/2298}}</ref> and in bovine prolactin mRNA (Horowitz et al 1984). In plants, the majority of the m<sup>6</sup>A is found within 150 nucleotides before the start of the [[poly(A) tail]]<ref name=Bodi2012>{{cite journal|last=Bodi, Z., Zhong, S., Mehra, S., Song, J., Graham, N., Li, H., May, S., Fray, R.G.|title=Adenosine methylation in Arabidopsis mRNA is associated with the 3′ end and reduced levels cause developmental defects|journal=Front. Plant Sci.|year=2012|volume=3|pages=48|url=http://www.frontiersin.org/Plant_Genetics_and_Genomics/10.3389/fpls.2012.00048/abstract}}</ref>.


In budding yeast (''Sacharomyces cerevisiae''), the [[homologue]] of [[METTL3]], IME4 is induced in diploid cells in response to nitrogen and fermentable carbon source starvation and is required for mRNA methylation and the initiation of correct meiosis and sporulation<ref name=Clancy2k2 /><ref name=Bodi2k10 />. mRNAs of IME1 and IME2, key early regulators of [[meiosis]], are known to be targets for [[methylation]], as are [[transcripts]] of IME4 itself<ref name=Bodi2k10 />.
⚫
m<sup>6</sup>A is susceptible to dynamic regulation both throughout development and in response to cellular stimuli. Analysis of m<sup>6</sup>A in mouse brain RNA reveals that m<sup>6</sup>A levels are low during embryonic development and increase dramatically by adulthood.<ref name=Meyer_etal_2012 /> Additionally, silencing the m<sup>6</sup>A [[methyltransferase]] significantly affects gene expression and alternative [[RNA splicing]] patterns, resulting in modulation of the [[p53]] (also known as [[TP53]]) signalling pathway and [[apoptosis]].<ref name=Dominissini2012 />


In plants, mutations of MTA, the ''[[Arabidopsis thaliana]]'' homologue of METTL3, results in [[embryo]] arrest at the globular stage. A >90% reduction of m<sup>6</sup>A levels in mature plants leads to dramatically altered growth patterns and floral homeotic abnormalities<ref name=Bodi2012 />.



⚫
The obesity risk gene, [[FTO gene | ''FTO'']], encodes the first identified m<sup>6</sup>A demethylase.<ref name=Jiaetal2011>{{cite journal|last=Jia|first=G|coauthors=Fu Y, Zhao X, Dai Q, Zheng G, Yang Y, Yi C, Lindahl T, Pan T, Yang YG, He C.|title=N6-methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO|journal=Nature Chemical Biology|date=16|year=2011|month=October|volume=7|issue=12|pages=885-7|doi=10.1038/nchembio.687|pmid=22002720|url=http://www.nature.com/nchembio/journal/v7/n12/full/nchembio.687.html}}</ref> <ref name=Meyer_etal_2012 /> [[FTO gene | ''FTO'']] mutations have been associated with increased risk for obesity and type 2 diabetes, which implicates m<sup>6</sup>A in important physiological pathways related to human disease. [[FTO gene | FTO]] [[knockdown]] with [[siRNA]] leads to increased amounts of m<sup>6</sup>A in [[polyA-RNA | poly(A) RNA]],<ref name=Dominissini2012 /> whereas [[overexpression]] of [[FTO gene | FTO]] results in decreased amounts of m<sup>6</sup>A in human cells.<ref name=Meyer_etal_2012 /> FTO partially localizes to [[nuclear speckles]],<ref name=Jiaetal2011 /> which supports the notion that m<sup>6</sup>A in nuclear RNA is a major physiological [[substrate]] of FTO. The consequences of FTO-guided demethylation are unknown, but it is likely to affect the processing of [[pre-mRNA]], other nuclear RNAs, or both. The discovery that FTO functions as a cellular m<sup>6</sup>A demethylase suggests that increased FTO activity in patients with ''FTO'' mutations leads to abnormally low levels of m<sup>6</sup>A in target mRNAs, which through as-yet undefined pathways contributes to the onset of obesity and related diseases.
Mapping of m<sup>6</sup>A in human and mouse RNA has identified over 18,000 m<sup>6</sup>A sites in the transcripts of more than 7,000 human genes with a [[consensus sequence]] of [G/A/U][G>A]m<sup>6</sup>AC[U>A/C]<ref name=Meyer_etal_2012 /> <ref name=Dominissini2012 /> consitent with the previously identified motif. The localization of individual m<sup>6</sup>A sites in many mRNAs is highly similar between [[human]] and [[mouse]],<ref name=Meyer_etal_2012 /> <ref name=Dominissini2012 /> and [[transcriptome]]-wide analysis reveals that m<sup>6</sup>A is found in regions of high [[evolutionary conservation]].<ref name=Meyer_etal_2012 /> m<sup>6</sup>A is found within long internal [[exons]] and is preferentially enriched within 3’ UTRs and around [[stop codons]]. m<sup>6</sup>A within 3’ UTRs is also associated with the presence of microRNA binding sites; roughly 2/3 of the mRNAs which contain an m<sup>6</sup>A site within their 3’ UTR also have at least one microRNA binding site.<ref name=Meyer_etal_2012 />

⚫
m<sup>6</sup>A is susceptible to dynamic regulation both throughout development and in response to cellular stimuli. Analysis of m<sup>6</sup>A in mouse brain RNA reveals that m<sup>6</sup>A levels are low during embryonic development and increase dramatically by adulthood.<ref name=Meyer_etal_2012 /> Additionally, silencing the m<sup>6</sup>A [[methyltransferase]] significantly affects gene expression and alternative [[RNA splicing]] patterns, resulting in modulation of the [[p53]] (also known as [[TP53]]) signalling pathway and [[apoptosis]].<ref name=Dominissini2012 />


⚫
The obesity risk gene, [[FTO gene | ''FTO'']], encodes the first identified m<sup>6</sup>A demethylase.<ref name=Jiaetal2011>{{cite journal|last=Jia|first=G|coauthors=Fu, Y., Zhao, X., Dai, Q., Zheng, G., Yang, Y., Yi, C., Lindahl, T., Pan, T., Yang, Y.G., He, C.|title=N6-methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO|journal=Nature Chemical Biology|date=16|year=2011|month=October|volume=7|pages=885-7|doi=10.1038/nchembio.687|pmid=22002720|url=http://www.nature.com/nchembio/journal/v7/n12/full/nchembio.687.html}}</ref> <ref name=Meyer_etal_2012 /> [[FTO gene | ''FTO'']] mutations have been associated with increased risk for obesity and type 2 diabetes, which implicates m<sup>6</sup>A in important physiological pathways related to human disease. [[FTO gene | FTO]] [[knockdown]] with [[siRNA]] leads to increased amounts of m<sup>6</sup>A in poly(A) RNA,<ref name=Dominissini2012 /> whereas [[overexpression]] of [[FTO gene | FTO]] results in decreased amounts of m<sup>6</sup>A in human cells.<ref name=Meyer_etal_2012 /> FTO partially localizes to [[nuclear speckles]],<ref name=Jiaetal2011 /> which supports the notion that m<sup>6</sup>A in nuclear RNA is a major physiological [[substrate]] of FTO. The consequences of FTO-guided demethylation are unknown, but it is likely to affect the processing of [[pre-mRNA]], other nuclear RNAs, or both. The discovery that FTO functions as a cellular m<sup>6</sup>A demethylase suggests that increased FTO activity in patients with ''FTO'' mutations leads to abnormally low levels of m<sup>6</sup>A in target mRNAs, which through as-yet undefined pathways contributes to the onset of obesity and related diseases.




Revision as of 22:42, 23 May 2012

N6-Methyladenosine
Names
IUPAC name
N-Methyladenosine
Other names
m6A
Identifiers
3D model (JSmol)
ChemSpider
  • InChI=1S/C11H15N5O4/c1-12-9-6-10(14-3-13-9)16(4-15-6)11-8(19)7(18)5(2-17)20-11/h3-5,7-8,11,17-19H,2H2,1H3,(H,12,13,14)/t5-,7-,8-,11-/m1/s1
    Key: VQAYFKKCNSOZKM-IOSLPCCCSA-N
  • InChI=1/C11H15N5O4/c1-12-9-6-10(14-3-13-9)16(4-15-6)11-8(19)7(18)5(2-17)20-11/h3-5,7-8,11,17-19H,2H2,1H3,(H,12,13,14)/t5-,7-,8-,11-/m1/s1
    Key: VQAYFKKCNSOZKM-IOSLPCCCBA
  • n2c1c(ncnc1NC)n(c2)[C@@H]3O[C@@H]([C@@H](O)[C@H]3O)CO
Properties
C11H15N5O4
Molar mass 281.272 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).


N6-Methyladenosine (m6A ) is an abundant modification in mRNA and is found within some viruses[1] [2], and most eukaryotes including mammals[3] [4] [5] [6], insects[7], plants[8][9][10] and yeast[11] [12]. It and is also found in tRNA, rRNA, and small nuclear RNA (snRNA) as well as several long non-coding RNA, such as Xist[13] [14].Adenosine methylation is directed by a large m6A methyltransferase complex containing METTL3 as the SAM-binding sub-unit [15] In vitro, this methyltransferase complex preferentially methylates RNA oligonucleotides containing GGACU[16] and a similar preference was identified in vivo in mapped m6A sites in Rous sarcoma virus genomic RNA[17] and in bovine prolactin mRNA (Horowitz et al 1984). In plants, the majority of the m6A is found within 150 nucleotides before the start of the poly(A) tail[18].

In budding yeast (Sacharomyces cerevisiae), the homologue of METTL3, IME4 is induced in diploid cells in response to nitrogen and fermentable carbon source starvation and is required for mRNA methylation and the initiation of correct meiosis and sporulation[11][12]. mRNAs of IME1 and IME2, key early regulators of meiosis, are known to be targets for methylation, as are transcripts of IME4 itself[12].

In plants, mutations of MTA, the Arabidopsis thaliana homologue of METTL3, results in embryo arrest at the globular stage. A >90% reduction of m6A levels in mature plants leads to dramatically altered growth patterns and floral homeotic abnormalities[18].


Mapping of m6A in human and mouse RNA has identified over 18,000 m6A sites in the transcripts of more than 7,000 human genes with a consensus sequence of [G/A/U][G>A]m6AC[U>A/C][13] [14] consitent with the previously identified motif. The localization of individual m6A sites in many mRNAs is highly similar between human and mouse,[13] [14] and transcriptome-wide analysis reveals that m6A is found in regions of high evolutionary conservation.[13] m6A is found within long internal exons and is preferentially enriched within 3’ UTRs and around stop codons. m6A within 3’ UTRs is also associated with the presence of microRNA binding sites; roughly 2/3 of the mRNAs which contain an m6A site within their 3’ UTR also have at least one microRNA binding site.[13]

m6A is susceptible to dynamic regulation both throughout development and in response to cellular stimuli. Analysis of m6A in mouse brain RNA reveals that m6A levels are low during embryonic development and increase dramatically by adulthood.[13] Additionally, silencing the m6A methyltransferase significantly affects gene expression and alternative RNA splicing patterns, resulting in modulation of the p53 (also known as TP53) signalling pathway and apoptosis.[14]


The obesity risk gene, FTO, encodes the first identified m6A demethylase.[19] [13] FTO mutations have been associated with increased risk for obesity and type 2 diabetes, which implicates m6A in important physiological pathways related to human disease. FTO knockdown with siRNA leads to increased amounts of m6A in poly(A) RNA,[14] whereas overexpression of FTO results in decreased amounts of m6A in human cells.[13] FTO partially localizes to nuclear speckles,[19] which supports the notion that m6A in nuclear RNA is a major physiological substrate of FTO. The consequences of FTO-guided demethylation are unknown, but it is likely to affect the processing of pre-mRNA, other nuclear RNAs, or both. The discovery that FTO functions as a cellular m6A demethylase suggests that increased FTO activity in patients with FTO mutations leads to abnormally low levels of m6A in target mRNAs, which through as-yet undefined pathways contributes to the onset of obesity and related diseases.


References

  1. ^ Aloni, Y., Dhar, R., and Khoury, G. (1979). "Methylation of nuclear simian virus 40 RNAs". J. Virol. 32: 52–60.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Beemon, K., Keith, J. (1977). "Localization of N6 methyladenosine in Rous sarcoma virus genome". J. Mol. Biol. 113: 165–179.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ Desrosiers, R.C., Friderici, K.H., Rottman F.M. (1974). "Identification of methylated nucleosides in messenger-RNA from Novikoff hepatoma cells". Proc. Natl. Acad Sci. 71: 3971–3975.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ Adams, J.M., and Cory, S. (1975). "Modified nucleosides and bizarre 5'-terminai in mouse myeloma mRNA". Nature. 255: 28–33.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  5. ^ Wei, C.M., Gershowitz, A., and Moss B. (1976). "5'-terminal and internal methylated nucleotide sequences in HeLa cell mRNA". Biochemistry. 15: 397–401.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  6. ^ Perry, R.P., Kelley, D.E., Fridirici, K., and Rottman, F.M. (1975). "The methylated constituents of L cell messenger RNA: evidence for an unsual cluster at the 5'-terminus". Cell. 4: 387–394.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  7. ^ Levis, R., and Penman, S. (1978). "5'-Terminal structures of poly(A)+ cytoplasmic messenger-RNA and of poly(A)+ and poly(A)- heterogeneous nuclear-RNA of cells of dipteran Drosophila-melanogaster". J. Mol. Bio. 120: 487–515.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  8. ^ Nichols, J.L. (1979). "N6-methyladenosine in maize poly(A)-containing RNA". Plant Science Letters. 15: 357–367.
  9. ^ Kennedy, T.D., and Lane, B.G. (1979). "Wheat embryo ribonucleates. XIII. Methyl-substituted nucleoside constituents and 5'-terminal dinucleotide sequences in bulk poly(A)-rich RNA from imbibing wheat embryos". Can. J. Biochem. 57: 927–931.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  10. ^ Zhong, S., Li, H., Bodi, Z., Button, J., Vespa, L., Herzog, M., Fray, R.G (2008). Plant Cell. 20: 1278–1288 http://www.plantcell.org/cgi/content/short/tpc.108.058883?keytype=ref&ijkey=tIrXWY7QkOJHRDz. {{cite journal}}: Missing or empty |title= (help)CS1 maint: multiple names: authors list (link)
  11. ^ a b Clancy, M.J., Shambaugh, M.E., Timpte, C.S., and Bokar, J.A. (2002). "Induction of sporulation in Saccharomyces cerevisiae leads to the formation of N6-methyladenosine in mRNA: a potential mechanism for the acivity of the IME4 gene". Nucleic Acids Res. 30: 4509–4518.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  12. ^ a b c Bodi, Z., Button, J.D., Grierson, D. and Fray, R.G. (2010). "Yeast targets for mRNA methylation". Nucleic Acids Research. 38: 5327–5335.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  13. ^ a b c d e f g h Meyer, KD. (2012). "Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3′ UTRs and near Stop Codons". Cell. doi:10.1016/j.cell.2012.05.003. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)
  14. ^ a b c d e Dominissini, D. "Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq". Nature. doi:10.1038/nature11112. {{cite journal}}: Unknown parameter |Year= ignored (|year= suggested) (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  15. ^ Bokar, JA (1997). "Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase". RNA. 3: 1233–47. PMC 1369564. PMID 9409616. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)
  16. ^ Harper, J.E., Miceli, S.M., Roberts R.J., and Manley, J.L. (1990). "). Sequence specificity of the human messenger-RNA N6-adenosine methylase in vitro". Nucleic Acids Res. 18: 5735–5741.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  17. ^ Kane, S.E., and Beemon, K. (1985). "Precise localization of m6A in Rous sarcoma virus RNA reveals clustering of methylation sites: Implications for RNA processing". Mol. Cell. Biol. 5: 2298–2306.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  18. ^ a b Bodi, Z., Zhong, S., Mehra, S., Song, J., Graham, N., Li, H., May, S., Fray, R.G. (2012). "Adenosine methylation in Arabidopsis mRNA is associated with the 3′ end and reduced levels cause developmental defects". Front. Plant Sci. 3: 48.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  19. ^ a b Jia, G (16). "N6-methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO". Nature Chemical Biology. 7: 885–7. doi:10.1038/nchembio.687. PMID 22002720. {{cite journal}}: Check date values in: |date= and |year= / |date= mismatch (help); Unknown parameter |coauthors= ignored (|author= suggested) (help); Unknown parameter |month= ignored (help)
Retrieved from "https://en.wikipedia.org/w/index.php?title=N6-Methyladenosine&oldid=494062728"