Purification, crystallization and preliminary crystallographic studies of C-terminal RNA recognition motif (RRM-3) of human ELAV-type RNA-binding protein 3 (ETR-3).

ABSTRACT: Human embryonically lethal abnormal vision (ELAV)-type RNA-binding protein 3 (ETR-3) has been implicated in many aspects of RNA-processing events including alternative splicing, stability, editing and translation. RNA recognition motif 3 (RRM-3) is an independent C-terminal RNA-binding domain of ETR-3 that preferentially binds to UG-rich repeats of the nuclear or cytoplasmic pre-mRNA, and along with the other domains mediates the inclusion of cardiac troponin T (c-TNT) exon 5 in embryonic muscle, which is otherwise excluded in the adult. In the present study, RRM-3 was cloned, overexpressed, purified and crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 3?Å resolution at the home source and belonged to space group P2?3, with unit-cell parameters a=b=c=118.5?Å, ?=?=?=90°. There were two molecules of RRM-3 in the asymmetric unit and the calculated Matthews coefficient (VM) was 6.35?Å3?Da(-1), with a solvent content of 80.62%. Initial phases were determined by molecular replacement.

SUBMITTER: Kashyap M 

PROVIDER: S-EPMC3792667 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature