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A tale of two reverse transcriptases – assembly, structural dynamics and function of telomerase and HIV reverse transcriptase
Author(s) -
Zhuang Xiaowei
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.399.2
Subject(s) - reverse transcriptase , dna , ribonucleoprotein , rna , biology , telomerase , nucleic acid , telomere , microbiology and biotechnology , chemistry , genetics , gene
Telomerase is a cellular ribonucleoprotein (RNP) that solves the end replication problem and maintains chromosome stability by adding telomeric DNA to the termini of linear chromosomes. It is a specialized reverse transcriptase (RT) that uses sequence encoded in its own RNA component as a template to synthesize telemetric DNA repeats. The RT of human immunodeficiency virus (HIV) is a viral protein that catalyzes an orchestrated series of reactions, including RNA‐directed DNA synthesis, DNA‐directed DNA synthesis and DNA‐directed RNA hydrolysis, to convert the single‐stranded RNA genome of HIV into double‐stranded DNA for host‐cell integration. Using single molecule FRET, we have investigated the assembly pathway, structural dynamics and structure‐function relation of these two RT systems. For both RT‐nucleic acid substrate complexes, novel assembly and structural dynamics were discovered that are critical for the enzymatic functions of these systems.