Importance of 5'-terminal blocking structure to stabilize mRNA in eukaryotic protein synthesis.

Shimotohno, Kunitada; Kodama, Yaeko; Hashimoto, Junji; Miura, Kiyonori

doi:10.1073/pnas.74.7.2734

Cited by 166 publications

(86 citation statements)

References 29 publications

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“…In addition, RNA gel blots of PHYA mRNA with high resolution NuSieve agarose gels, similar to those used in the RNase H analyses (Figures 3 and S), detected the continuous distribution of PHYA fragments but failed to detect discrete degradation products (data not shown). This does not rule out the possibility of a stochastic endoribonuclease activity, but a 5l-3' exoribonuclease seems more likely to degrade PHYA mRNA because similar enzymes are reported to be involved in the degradation of plant mRNAs (Shimotohno et al, 1977) and other eukaryotic mRNAs (Furuichi et al, 1977;Stevens, 1980;Stevens and Maupin, 1987;Vreken and Rau6, 1992).…”

Section: Discussionmentioning

confidence: 99%

“…Such ribonuclease activities are reported in Xenopus oocytes and mouse L cells (Furuichi et al, 1977), yeast cells (Stevens, 1980;Vreken and Rau6, 1992), human placenta1 nuclei (Stevens and Maupin, 1987), and wheat germ extracts (Shimotohno et al, 1977). Two 5l-3' exoribonucleases (XRN1 and HKEllRATl) have been cloned from yeast cells (Larimer et al, 1992;Kenna et al, 1993).…”

Section: Discussionmentioning

confidence: 99%

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Oat phytochrome A mRNA degradation appears to occur via two distinct pathways.

Higgs

Colbert

1994

Plant Cell

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Oat phytochrome A mRNA degradation appears to occur via two distinct pathways.

Higgs

Colbert

1994

Plant Cell

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“…The m 7 G cap modulates numerous facets of mRNA metabolism, including stability (12,13), translation (14,15), and export (16). The importance of this modification is underscored by the substantial cellular machinery dedicated to its addition and removal (17,18).…”

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confidence: 99%

Identification of NAD ⁺ capped mRNAs in Saccharomyces cerevisiae

Walters

Matheny

Mizoue

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

122

161

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RNAs besides tRNA and rRNA contain chemical modifications, including the recently described 5′ nicotinamide-adenine dinucleotide (NAD + ) RNA in bacteria. Whether 5′ NAD-RNA exists in eukaryotes remains unknown. We demonstrate that 5′ NAD-RNA is found on subsets of nuclear and mitochondrial encoded mRNAs in Saccharomyces cerevisiae. NAD-mRNA appears to be produced cotranscriptionally because NAD-RNA is also found on pre-mRNAs, and only on mitochondrial transcripts that are not 5′ end processed. These results define an additional 5′ RNA cap structure in eukaryotes and raise the possibility that this 5′ NAD + cap could modulate RNA stability and translation on specific subclasses of mRNAs.T he number and prevalence of known chemical modifications on mRNAs have dramatically increased in the past several years (1). Quantification of these modification events suggests they occur in many RNAs (2, 3). Importantly, several of these modifications have functional consequences (4-6). For example, the presence of a single N 6 -methyladenosine within the 5′ UTR of an mRNA increases translation initiation (4). In addition, the methylation status of cytosine residues within the 3′ UTR of the p16(INK4) human mRNA affects mRNA stability (6). Due to the increasing sensitivity of RNA sequencing (RNA-Seq) and small-molecule mass spectrometry, it is reasonable to hypothesize that many novel chemical modifications within mRNAs remain to be discovered.One modification recently identified in bacteria is 5′ nicotinamide-adenine dinucleotide (NAD + )-linked RNA (7, 8). Because canonical bacterial RNAs contain a 5′ triphosphate terminus, addition of NAD + to the 5′ end of RNAs represents a rudimentary "capping" mechanism, perhaps designed to impart specific properties for these RNAs by granting them a more structurally complex 5′ end. Consistent with this idea, NAD + addition to RNAs appears to occur during transcription initiation (9), as opposed to the more complex eukaryote 5′ capping, which occurs after transcription has commenced (10). Because the NAD + modification defines the 5′ end of NAD-RNAs, this modification can affect RNA stability in Escherichia coli (7, 9).For decades, 5′ end classification and study of eukaryotic mRNAs have been restricted to canonical 7-methylguanosine (m 7 G) "caps" and their methylated variants (11). The m 7 G cap modulates numerous facets of mRNA metabolism, including stability (12, 13), translation (14, 15), and export (16). The importance of this modification is underscored by the substantial cellular machinery dedicated to its addition and removal (17,18). Thus, mRNAs containing noncanonical 5′ termini may have distinct properties and be subject to alternative metabolic events.Described herein is the identification of NAD-RNAs in the eukaryote Saccharomyces cerevisiae. Examples of NAD-RNAs in S. cerevisiae include nuclear encoded mRNAs for ribosomal proteins, as well as some mitochondrial encoded transcripts. Our data suggest that the NAD + moiety is added during initiation in both nuclear and mitoc...

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“…Radioautography was done as described (20). Except where indicated, all S-10 extracts from infected cells were prepared from L cells that had been infected with reovirus at a multiplicity of 5 (21)(22)(23). Fig.…”

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confidence: 99%

Reovirus-induced modification of cap-dependent translation in infected L cells.

Skup¹,

Millward²

1980

Proc. Natl. Acad. Sci. U.S.A.

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The translational apparatus in cell-free extracts prepared from L cells infected with reovirus undergoes a time-dependent transition from cap dependence to cap independence. Extracts from uninfected L cells translate capped reovirus mRNA at high efficiency and synthesize the expected three size classes of reovirus polypeptides, and the translation is sensitive to m7G(5')ppp. This same extract translates uncapped mRNA at a much lower efficiency. In contrast, extracts from infected L cells translate uncapped reovirus mRNA at high efficiency and synthesize the correct three size classes of polypeptides, and the translation is not sensitive to inhibition by m7G(5')ppp. Infected cell extracts translate capped mRNA at reduced efficiency (z25%), the translation is not sensitive to inhibition by m7G(5')ppp, and the correct three size classes of viral polypeptides are not synthesized. These observations may explain how reovirus takes over the host translational apparatus.the viral mRNA in this process. The recent development of a method for making efficient cell-free protein-synthesizing systems of extremely low background activity from L cells (14) has enabled us to compare the in vitro translation of exogenously supplied reovirus mRNA in extracts that have been prepared from infected and uninfected L cells. Using extracts from infected cells, we found that the translation of uncapped reovirus mRNA is highly efficient and that the ability of these extracts to translate this form of reovirus mRNA increases with time of infection. Our observations lead us to conclude that the host cell translational machinery becomes modified as a result of viral infection. A model is proposed for the reovirus-induced takeover of the host cell translation machinery, in which uncapped viral mRNAs are preferentially translated at late times during infection.

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Importance of 5'-terminal blocking structure to stabilize mRNA in eukaryotic protein synthesis.

Cited by 166 publications

References 29 publications

Oat phytochrome A mRNA degradation appears to occur via two distinct pathways.

Oat phytochrome A mRNA degradation appears to occur via two distinct pathways.

Identification of NAD ⁺ capped mRNAs in Saccharomyces cerevisiae

Reovirus-induced modification of cap-dependent translation in infected L cells.

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Importance of 5'-terminal blocking structure to stabilize mRNA in eukaryotic protein synthesis.

Cited by 166 publications

References 29 publications

Oat phytochrome A mRNA degradation appears to occur via two distinct pathways.

Oat phytochrome A mRNA degradation appears to occur via two distinct pathways.

Identification of NAD + capped mRNAs in Saccharomyces cerevisiae

Reovirus-induced modification of cap-dependent translation in infected L cells.

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Identification of NAD ⁺ capped mRNAs in Saccharomyces cerevisiae