Analysis of telomerase processivity: mechanistic similarity to HIV-1 reverse transcriptase and role in telomere maintenance.
The key protein subunit of the telomerase complex, known as TERT, possesses a reverse transcriptase (RT)-like domain that is conserved in enzymes encoded by retroviruses and retroelements. Structural and functional analysis of HIV-1 RT suggests that RT processivity is governed, in part, by the conserved motif C, motif E, and a C-terminal domain. Mutations in analogous regions of the yeast TERT were found to have anticipated effects on telomerase processivity in vitro, suggesting a great deal of mechanistic and structural similarity between TERT and retroviral RTs, and a similarity that goes beyond the homologous domain. A close correlation was uncovered between telomerase processivity and telomere length in vivo, suggesting that enzyme processivity is a limiting factor for telomere maintenance.
Peng
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Department of Microbiology and Immunology, W. R. Hearst Microbiology Research Center, Weill Medical College, Cornell University, 10021, New York, NY, USA.
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D020134:Catalytic Domain; D004268:DNA-Binding Proteins; D054303:HIV Reverse Transcriptase / Q000378:metabolism*; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D016296:Mutagenesis; D012313:RNA; D017386:Sequence Homology, Amino Acid; D019098:Telomerase / Q000378:metabolism*; D016615:Telomere / Q000201:enzymology*; D015003:Yeasts
D004268:DNA-Binding Proteins; C034477:RNA primers; C422952:telomerase RNA; D012313:RNA; D054303:HIV Reverse Transcriptase; D019098:Telomerase