In vitro selection of N peptide-binding RNA on a quartz-crystal microbalance
Author(s) -
Akiko Murakawa,
Shinobu Fukusho,
Hiroyuki Furusawa,
Yoshio Okahata
Publication year - 2002
Publication title -
nucleic acids symposium series
Language(s) - English
Resource type - Journals
eISSN - 1746-8272
pISSN - 0261-3166
DOI - 10.1093/nass/2.1.207
Subject(s) - quartz crystal microbalance , rna , peptide , rna binding protein , chemistry , binding site , systematic evolution of ligands by exponential enrichment , in vitro , peptide library , microbiology and biotechnology , peptide sequence , biochemistry , biology , gene , adsorption , organic chemistry
We report here an in vitro selection of a hairpin loop-RNA bound to N Peptide from bacteriophage lambda on a 27 MHz quartz-crystal microbalance (QCM) to study an interaction between an RNA structure and an RNA-binding peptide. The N Peptide was immobilized on a QCM electrode and specific RNAs binding to the peptide were selected from a GNRNA pentaloop-randomized RNA library with in situ monitoring of selection processes using a QCM. After the 5th round selection, the consensus sequences including a GCGCA loop were obtained from the pentaloop library. This RNA sequence was different from a binding site of a native N Protein (boxB RNA).
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom