BROWSE

Related Scientist

Vladimir, Reinharz's photo.

Vladimir, Reinharz
첨단연성물질 연구단
more info

ITEM VIEW & DOWNLOAD

αβDCA method identifies unspecific binding but specific disruption of the group I intron by the StpA chaperone

Cited 0 time in webofscience Cited 0 time in scopus
20 Viewed 0 Downloaded
Title
αβDCA method identifies unspecific binding but specific disruption of the group I intron by the StpA chaperone
Author(s)
REINHARZ, VLADIMIR; Tlusty, Tsvi
Publication Date
2020-11
Journal
RNA, v.26, no.11, pp.1530 - 1540
Publisher
Cold Spring Harbor Laboratory Press
Abstract
© 2020 Cold Spring Harbor Laboratory Press. All rights reserved.Chaperone proteins-the most disordered among all protein groups-help RNAs fold into their functional structure by destabilizing misfolded configurations or stabilizing the functional ones. But disentangling the mechanism underlying RNA chaperoning is challenging, mostly because of inherent disorder of the chaperones and the transient nature of their interactions with RNA. In particular, it is unclear how specific the interactions are and what role is played by amino acid charge and polarity patterns. Here, we address these questions in the RNA chaperone StpA. We adapted direct coupling analysis (DCA) into the αβDCA method that can treat in tandem sequences written in two alphabets, nucleotides and amino acids. With αβDCA, we could analyze StpA-RNA interactions and show consistency with a previously proposed two-pronged mechanism: StpA disrupts specific positions in the group I intron while globally and loosely binding to the entire structure. Moreover, the interactions are strongly associated with the charge pattern: Negatively charged regions in the destabilizing StpA amino-terminal affect a fewspecific positions in the RNA, located in stems and in the pseudoknot. In contrast, positive regions in the carboxy-terminal contain strongly coupled amino acids that promote nonspecific or weakly specific binding to the RNA. The present study opens new avenues to examine the functions of disordered proteins and to design disruptive proteins based on their charge patterns
URI
https://pr.ibs.re.kr/handle/8788114/9118
DOI
10.1261/rna.074336.119
ISSN
1355-8382
Appears in Collections:
Center for Soft and Living Matter(첨단연성물질 연구단) > 1. Journal Papers (저널논문)
Files in This Item:
There are no files associated with this item.

qrcode

  • facebook

    twitter

  • Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse