Unknown

Dataset Information

0

High-resolution NMR analysis of the conformations of native and base analog substituted retroviral and LTR-retrotransposon PPT primers.


ABSTRACT: A purine-rich region of the plus-strand RNA genome of retroviruses and long terminal repeat (LTR)-containing retrotransposons, known as the polypurine tract (PPT), is resistant to hydrolysis by the RNase H domain of reverse transcriptase (RT) and ultimately serves as a primer for plus-strand DNA synthesis. The mechanisms underlying PPT resistance and selective processing remain largely unknown. Here, two RNA/DNA hybrids derived from the PPTs of HIV-1 and Ty3 were probed using high-resolution NMR for preexisting structural distortions in the absence of RT. The PPTs were selectively modified through base-pair changes or by incorporation of the thymine isostere, 2,4-difluoro-5-methylbenzene (dF), into the DNA strand. Although both wild-type (WT) and mutated hybrids adopted global A-form-like helical geometries, observed structural perturbations in the base-pair and dF-modified hybrids suggested that the PPT hybrids may function as structurally coupled domains.

SUBMITTER: Yi-Brunozzi HY 

PROVIDER: S-EPMC2729084 | biostudies-literature | 2008 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

High-resolution NMR analysis of the conformations of native and base analog substituted retroviral and LTR-retrotransposon PPT primers.

Yi-Brunozzi Hye Young HY   Brinson Robert G RG   Brabazon Danielle M DM   Lener Daniela D   Le Grice Stuart F J SF   Marino John P JP  

Chemistry & biology 20080301 3


A purine-rich region of the plus-strand RNA genome of retroviruses and long terminal repeat (LTR)-containing retrotransposons, known as the polypurine tract (PPT), is resistant to hydrolysis by the RNase H domain of reverse transcriptase (RT) and ultimately serves as a primer for plus-strand DNA synthesis. The mechanisms underlying PPT resistance and selective processing remain largely unknown. Here, two RNA/DNA hybrids derived from the PPTs of HIV-1 and Ty3 were probed using high-resolution NMR  ...[more]

Similar Datasets

| S-EPMC5406212 | biostudies-literature
| S-EPMC147500 | biostudies-other
| S-EPMC5551035 | biostudies-literature
| S-EPMC3350952 | biostudies-literature
| S-EPMC307637 | biostudies-literature
| S-EPMC4054100 | biostudies-literature
| S-EPMC5333098 | biostudies-literature
| S-EPMC7081582 | biostudies-literature
| S-EPMC2040900 | biostudies-literature
| S-EPMC8396678 | biostudies-literature