Skip to main content
NCBI home page
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1995 Aug 11;23(15):2811–2814. doi: 10.1093/nar/23.15.2811

Reverse transcriptase reads through a 2'-5'linkage and a 2'-thiophosphate in a template.

J R Lorsch 1, D P Bartel 1, J W Szostak 1
PMCID: PMC307115  PMID: 7544885

Abstract

Avian myeloblastosis virus and Maloney murine leukemia virus RNase H-reverse transcriptases pause when they encounter a 2'-5' linkage or a 2'-thiophosphate in their template RNAs, but eventually read through these backbone modifications. Both reverse transcriptases pause after the 2'-5' linkage but before the 2'-thiophosphate. These results suggest that in the absence of precise information concerning the behavior of a given reverse transcriptase with respect to a particular lesion or modification, caution should be exercised in the interpretation of primer extension data that is being used to determine the existence of, or map the position of, a crosslink, site of chemical modification or non-standard linkage in an RNA template.

Full text

PDF
2811

Images in this article

2813Image
on p.2813

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bakhanashvili M., Hizi A. Fidelity of the RNA-dependent DNA synthesis exhibited by the reverse transcriptases of human immunodeficiency virus types 1 and 2 and of murine leukemia virus: mispair extension frequencies. Biochemistry. 1992 Oct 6;31(39):9393–9398. doi: 10.1021/bi00154a010. [DOI] [PubMed] [Google Scholar]
  2. Bartel D. P., Szostak J. W. Isolation of new ribozymes from a large pool of random sequences [see comment]. Science. 1993 Sep 10;261(5127):1411–1418. doi: 10.1126/science.7690155. [DOI] [PubMed] [Google Scholar]
  3. Denman R., Colgan J., Nurse K., Ofengand J. Crosslinking of the anticodon of P site bound tRNA to C-1400 of E.coli 16S RNA does not require the participation of the 50S subunit. Nucleic Acids Res. 1988 Jan 11;16(1):165–178. doi: 10.1093/nar/16.1.165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Domdey H., Apostol B., Lin R. J., Newman A., Brody E., Abelson J. Lariat structures are in vivo intermediates in yeast pre-mRNA splicing. Cell. 1984 Dec;39(3 Pt 2):611–621. doi: 10.1016/0092-8674(84)90468-9. [DOI] [PubMed] [Google Scholar]
  5. Lorsch J. R., Szostak J. W. In vitro evolution of new ribozymes with polynucleotide kinase activity. Nature. 1994 Sep 1;371(6492):31–36. doi: 10.1038/371031a0. [DOI] [PubMed] [Google Scholar]
  6. Mendelman L. V., Petruska J., Goodman M. F. Base mispair extension kinetics. Comparison of DNA polymerase alpha and reverse transcriptase. J Biol Chem. 1990 Feb 5;265(4):2338–2346. [PubMed] [Google Scholar]
  7. Mörl M., Niemer I., Schmelzer C. New reactions catalyzed by a group II intron ribozyme with RNA and DNA substrates. Cell. 1992 Sep 4;70(5):803–810. doi: 10.1016/0092-8674(92)90313-2. [DOI] [PubMed] [Google Scholar]
  8. Rodriguez J. R., Pikielny C. W., Rosbash M. In vivo characterization of yeast mRNA processing intermediates. Cell. 1984 Dec;39(3 Pt 2):603–610. doi: 10.1016/0092-8674(84)90467-7. [DOI] [PubMed] [Google Scholar]
  9. Youvan D. C., Hearst J. E. Reverse transcriptase pauses at N2-methylguanine during in vitro transcription of Escherichia coli 16S ribosomal RNA. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3751–3754. doi: 10.1073/pnas.76.8.3751. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Zeitlin S., Efstratiadis A. In vivo splicing products of the rabbit beta-globin pre-mRNA. Cell. 1984 Dec;39(3 Pt 2):589–602. doi: 10.1016/0092-8674(84)90466-5. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES