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RNA aptamers that specifically bind to the Ras‐binding domain of Raf‐1
Author(s) -
Kimoto Michiko,
Sakamoto Kensaku,
Shirouzu Mikako,
Hirao Ichiro,
Yokoyama Shigeyuki
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01572-5
Subject(s) - aptamer , rna , binding domain , chemistry , dissociation constant , microbiology and biotechnology , binding site , selex aptamer technique , biology , riboswitch , rna binding protein , plasma protein binding , biochemistry , non coding rna , systematic evolution of ligands by exponential enrichment , gene , receptor
RNA aptamers that bind to the Ras‐binding domain (RBD) of a proto‐oncogene product, Raf‐1, were isolated from a pool of random sequences using a glutathione S ‐transferase‐fused RBD (GST‐RBD). The RNA molecules bind to the GST‐RBD, but not to GST, with dissociation constants of about 300 nM. In contrast, these RNA aptamers do not bind to the Ras‐binding domain of the RGL protein, which is also known to be activated by Ras. The aptamers actually compete with Ras for binding to the Raf‐1 RBD. The anti‐Raf‐1 aptamers may be used to specifically inhibit the Ras‐Raf interaction in the complicated signaling network in mammalian cells.