id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-001453-l1r416w7	Hou, Linlin	Archaeal DnaG contains a conserved N-terminal RNA-binding domain and enables tailing of rRNA by the exosome	2014-11-10		.txt	text/plain	8358	420	54	title: Archaeal DnaG contains a conserved N-terminal RNA-binding domain and enables tailing of rRNA by the exosome Consistently, a fusion protein containing full-length Csl4 and NTD of DnaG led to enhanced degradation of A-rich RNA by the exosome. The RNase PH-domain containing subunits Rrp41 and Rrp42 are arranged in a catalytically active hexamer, on the top of which a trimeric cap composed of the RNA-binding proteins Rrp4 and Csl4 is bound ( Figure 1B ; 4, 5, [22] [23] [24] . The bacterial primase DnaG is composed of an NTD containing a Zn-finger motif involved in DNA binding, the central, catalytic TOPRIM domain and a CTD neces-sary for the interaction with the replicative helicase DnaB ( Figure 1A , refs. coli cell-free extract was easily detectable by pull-down assays with Strep-Tactin Sepharose beads (for an example see Figure 7A be-low), we conclude that the CTD of DnaG is important for the binding to the archaeal exosome.	./cache/cord-001453-l1r416w7.txt	./txt/cord-001453-l1r416w7.txt