|Analysis of telomerase processivity: mechanistic similarity to HIV-1 reverse transcriptase and role in telomere maintenance.
|Year of Publication
|Peng Y, Mian IS, Lue NF
|Catalytic Domain, DNA-Binding Proteins, HIV Reverse Transcriptase, In Vitro Techniques, Molecular Sequence Data, Mutagenesis, RNA, Sequence Homology, Amino Acid, Telomerase, Telomere, Yeasts
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.
Submitted by jom4013 on December 3, 2020 - 4:18pm