-globin mRNAs capped with m7G, m22.7G or m32.2.7G differ in intrinsic translation efficiency

Darżynkiewicz, Edward; Stępiński, Janusz; Ekiel, Irena; Jin, Youxin; Haber, Dorota; Sijuwade, Teju; Tahara, Stanley M.

doi:10.1093/nar/16.18.8953

Cited by 88 publications

(58 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…There is some concern that if an RNA has a TMG cap instead of an m7G cap, this could have repercussions for the initiation of translation. The proportion of hypermethylated guanosine-capped RNAs was found to be lower in polysomal RNA than in nonpolysomal RNA, suggesting that TMG RNAs may not be translated efficiently (57,58). How these in vitro findings reflect in vivo translation is not entirely clear, however.…”

Section: Discussionmentioning

confidence: 97%

Trimethylguanosine capping selectively promotes expression of Rev-dependent HIV-1 RNAs

Yedavalli

Jeang

2010

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

View full text Add to dashboard Cite

5′-mRNA capping is an early modification that affects pre-mRNA synthesis/splicing, RNA cytoplasmic transport, and mRNA translation and turnover. In eukaryotes, a 7-methylguanosine (m7G) cap is added to newly transcribed RNA polymerase II (RNAP II) transcripts. A subset of RNAP II-transcribed cellular RNAs, including small nuclear RNA (snRNA), small nucleolar RNA (snoRNA), and telomerase RNA, is further hypermethylated at the exocyclic N2 of the guanosine to create a trimethylguanosine (TMG)-capped RNA. Some of these TMG-capped RNAs are transported within the nucleus and from the nucleus to the cytoplasm by the CRM-1 (required for chromosome region maintenance) protein. CRM-1 is also used to export Rev/RRE-dependent unspliced/ partially spliced HIV-1 RNAs. Here we report that like snRNAs and snoRNAs, some Rev/RRE-dependent HIV-1 RNAs are TMG-capped. The methyltransferase responsible for TMG modification of HIV-1 RNAs is the human PIMT (peroxisome proliferator-activated receptor-interacting protein with methyltransferase) protein. TMG capping of unspliced/partially spliced HIV-1 RNAs represents a new regulatory mechanism for selective expression.required for chromosome region maintenance | RNA export | peroxisome proliferator-activated receptor-interacting protein with methyltransferase P osttranscriptional processing of RNA plays a critical role in gene expression (1-3). An early mRNA modification is the formation of a 7-methylguanosine (m7G) cap (4-6). In mammals, the acquisition of an m7G cap requires two enzymes (7-9), a capping enzyme (triphosphatase and guanylyltransferase activity) and an RNA-(guanine 7)-methyltransferase. These proteins are essential for cell growth, and mutations in the triphosphatase, guanylyltransferase, or methyltransferase components of the capping apparatus are lethal in vivo (10).Cellular RNAP II transcripts are mostly m7G-capped (1-3, 11). An m7G cap facilitates the initiation of translation in mammalian cells, and a failure to cap premRNAs results in their accelerated decay by 5′ exoribonuclease degradation (2,(12)(13)(14). Capping of viral RNAs has been less extensively investigated. It has been generally assumed that like cellular RNAs, many viral RNAs have a 5′ m7G cap, and that viruses either use the cellular capping machinery (e.g., viruses that replicate in the nucleus) or encode their own capping enzymes (e.g., viruses that replicate in the cytoplasm) (15, 16). Interestingly, there is a surprisingly diverse range of cap modifications; for instance, Mimivirus, a large DNA virus of amoeba, encodes an RNA cap guanine-N2 methyltransferase that hypermethylates the viral RNA cap (17); influenza virus "snatches" caps from cellular mRNAs (18, 19); West Nile fever virus has two methyl additions on its RNA cap (20); Sindbis virus produces mRNAs that have dimethylguanosine and trimethylguanosine caps [hypermethylated caps/m 2,2,7 G caps (21)]; and Semliki forest virus late mRNAs also have hypermethylated caps (22). On the other hand, poliovirus, encephalomyelitis virus, foot and mouth...

show abstract

Section: Discussionmentioning

confidence: 97%

Trimethylguanosine capping selectively promotes expression of Rev-dependent HIV-1 RNAs

Yedavalli

Jeang

2010

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

View full text Add to dashboard Cite

show abstract

“…Gp 3 G are translated in a rabbit reticulocyte system 1.5-fold more efficiently than m 7 Gp 3 G-capped mRNAs (Darzynkiewicz et al 1988). Similarly, mRNAs containing the bulky benzyl group on N7 (bn 7 Gp 3 G) instead of methyl are translated 1.7-fold more efficiently than mRNAs capped with the natural structure (Darzynkiewicz et al 1989).…”

Section: Discussionmentioning

confidence: 99%

Novel “anti-reverse” cap analogs with superior translational properties

Jemielity

Fowler²,

Zuberek³

et al. 2003

RNA

235

275

View full text Add to dashboard Cite

show abstract

“…As shown in Figure 2B, trans-spliced products are present in both the supernatant and the pellet. The poor precipitation of the trans-spliced product is likely attributable to the fact that it contains a trimethylguanosine cap (Liou et al 1990) that binds less efficiently to mammalian eIF4E (Darzynkiewicz et al 1988). In contrast, Ur-RNA is not detected at all in the pellet, suggesting it does not contain a 5Ј cap.…”

Section: Wwwrnajournalorgmentioning

confidence: 99%

An uncapped RNA suggests a model for Caenorhabditis elegans polycistronic pre-mRNA processing

Liu

Kuersten²,

Huang³

et al. 2003

RNA

View full text Add to dashboard Cite

Polycistronic pre-mRNAs from Caenohabditis elegans operons are processed by internal cleavage and polyadenylation to create 3' ends of mature mRNAs. This is accompanied by trans-splicing with SL2 ∼100 nucleotides downstream of the 3' end formation sites to create the 5' ends of downstream mRNAs. SL2 trans-splicing depends on a U-rich element (Ur), located ∼70 nucleotides upstream of the trans-splice site in the intercistronic region (ICR), as well as a functional 3 end formation signal. Here we report the existence of a novel gene-length RNA, the Ur-RNA, starting just upstream of the Ur element. The expression of Ur-RNA is dependent on 3 end formation as well as on the presence of the Ur element, but does not require a trans-splice site. The Ur-RNA is not capped, and alteration of the location of the Ur element in either the 5 or 3 direction alters the location of the 5 end of the Ur-RNA. We propose that a 5' to 3' exonuclease degrades the precursor RNA following cleavage at the poly(A) site, stopping when it reaches the Ur element, presumably attributable to a bound protein. Part of the function of this protein can be performed by the MS2 coat protein. Recruitment of coat protein to the ICR in the absence of the Ur element results in accumulation of an RNA equivalent to Ur-RNA, and restores trans-splicing. Only SL1, however, is used. Therefore, coat protein is sufficient for blocking the exonuclease and thereby allowing formation of a substrate for trans-splicing, but it lacks the ability to recruit the SL2 snRNP. Our results also demonstrate that MS2 coat protein can be used as an in vivo block to an exonuclease, which should have utility in mRNA stability studies.

show abstract

-globin mRNAs capped with m7G, m22.7G or m32.2.7G differ in intrinsic translation efficiency

Cited by 88 publications

References 40 publications

Trimethylguanosine capping selectively promotes expression of Rev-dependent HIV-1 RNAs

Trimethylguanosine capping selectively promotes expression of Rev-dependent HIV-1 RNAs

Novel “anti-reverse” cap analogs with superior translational properties

An uncapped RNA suggests a model for Caenorhabditis elegans polycistronic pre-mRNA processing

Contact Info

Product

Resources

About