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Publication Abstract from PubMed

Telomerase is a ribonucleoprotein complex essential for maintenance of telomere DNA at linear chromosome ends. The catalytic core of Tetrahymena telomerase comprises a ternary complex of telomerase RNA (TER), telomerase reverse transcriptase (TERT), and the essential La family protein p65. NMR and crystal structures of p65 C-terminal domain and its complex with stem IV of TER reveal that RNA recognition is achieved by a combination of single- and double-stranded RNA binding, which induces a 105 degrees bend in TER. The domain is a cryptic, atypical RNA recognition motif with a disordered C-terminal extension that forms an alpha helix in the complex necessary for hierarchical assembly of TERT with p65-TER. This work provides the first structural insight into biogenesis and assembly of TER with a telomerase-specific protein. Additionally, our studies define a structurally homologous domain (xRRM) in genuine La and LARP7 proteins and suggest a general mode of RNA binding for biogenesis of their diverse RNA targets.

Structural Basis for Telomerase RNA Recognition and RNP Assembly by the Holoenzyme La Family Protein p65.,Singh M, Wang Z, Koo BK, Patel A, Cascio D, Collins K, Feigon J Mol Cell. 2012 Jun 14. PMID:22705372^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.