Prognostic and Diagnostic Significance of Survivin


KAFADAR D.

Third International Congress of Molecular Medicine, 5 - 08 Mayıs 2009, cilt.61, ss.335, (Özet Bildiri) identifier identifier

  • Yayın Türü: Bildiri / Özet Bildiri
  • Cilt numarası: 61
  • Doi Numarası: 10.1002/iub.160
  • Sayfa Sayıları: ss.335
  • Anahtar Kelimeler: RNase P ribozyme, divalent metal ions, tRNA precursors, tRNAprocessing, METAL-ION BINDING, PRECURSOR TRANSFER-RNA, PHENYLALANINE TRANSFER-RNA, PYROCOCCUS-HORIKOSHII OT3, ARCHAEAL RIBONUCLEASE-P, PRE-TRANSFER RNAS, ESCHERICHIA-COLI, CRYSTAL-STRUCTURE, ACTIVE-SITE, M1 RNA
  • İstanbul Üniversitesi-Cerrahpaşa Adresli: Hayır

Özet

Metal(II)-induced hydrolysis of RNA produce products with 5'-hydroxyls and 2';3'-cyclic phosphates at the ends. Ribozymes are RNA molecules that act as catalysts. Some ribozymes that cleave RNA also generate 5-hydroxyls and 2';3-cyclic phosphates whereas others produces 5-phosphates and 5'-hydroxyls at the ends of the cleavage products. RNase P is an essential endoribonuclease involved in RNA processing. The catalytic RNA subunit or RNase P is a trans-acting ribozyme that cleaves various RNA substrates in vitro generating 5'-phosphates and Y-hydroxyls as cleavage products. The activity depends on the presence of metal(II) ions such as Mg2+. RNase P RNA has therefore to facilitate a nucleophilic attack that generates the correct product ends and prevent metal(II)-induced hydrolysis of the RNA substrate. In this review, we will discuss our current understanding of the interactions between RNase P RNA and its substrate, role of specific residues with respect to catalysis and positioning of functionally important Mg2+ at and in the vicinity of the cleavage site that ensures that products with correct ends are generated. Moreover, we will discuss the composition of RNase P and its RNA subunit in an evolutionary perspective. (C) 2009 IUBMB