Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Jorjethe Roca"'
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
Bacterial sRNAs compete for limited copies of an RNA chaperone. Here, real-time single-molecule imaging shows that pairwise interactions of sRNAs with Hfq determine if the sRNAs are actively exchanged or stably coexist on the shared protein.
Externí odkaz:
https://doaj.org/article/69a2f5a1e13f4692b75a6d372c1092f8
Publikováno v:
J Mol Biol
The Sm protein Hfq chaperones small non-coding RNAs (sRNAs) in bacteria, facilitating sRNA regulation of target mRNAs. Hfq acts in part by remodeling the sRNA and mRNA structures, yet the basis for this remodeling activity is not understood. To under
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4c2051ee8775dcea9e80b3052ab74fd
https://europepmc.org/articles/PMC10044511/
https://europepmc.org/articles/PMC10044511/
Autor:
Samantha H. Sarni, Jorjethe Roca, Chen Du, Mengxuan Jia, Hantian Li, Ana Damjanovic, Ewelina M. Małecka, Vicki H. Wysocki, Sarah A. Woodson
RNA-binding proteins contain intrinsically disordered regions whose functions in RNA recognition are poorly understood. The RNA chaperone Hfq is a homohexamer that contains six flexible C-terminal domains (CTDs). The effect of the CTDs on Hfq’s int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3675a61cb0e5842187d8cb2dc79d617
https://doi.org/10.1101/2022.05.23.493136
https://doi.org/10.1101/2022.05.23.493136
Publikováno v:
J Biol Phys
Pseudoknotted RNA molecules play important biological roles that depend on their folded structure. To understand the underlying principles that determine their thermodynamics and folding/unfolding mechanisms, we carried out a study on a variant of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ad65060f7515c73c0830a17a8d88b16
https://europepmc.org/articles/PMC9054998/
https://europepmc.org/articles/PMC9054998/
Publikováno v:
Nature communications. 13(1)
Hundreds of bacterial small RNAs (sRNAs) require the Hfq chaperone to regulate mRNA expression. Hfq is limiting, thus competition among sRNAs for binding to Hfq shapes the proteomes of individual cells. To understand how sRNAs compete for a common pa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f92a11a190517cb5223b7c9638a0db1c
https://pubmed.ncbi.nlm.nih.gov/35508531
https://pubmed.ncbi.nlm.nih.gov/35508531
Autor:
Saroj Baral, Prasanth Narayanan, Jorjethe Roca, D. Thirumalai, Ranjani Narayanan, Anjum Ansari, Naoto Hori, Yogambigai Velmurugu
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance The assembly mechanism of RNA, vital to describing its functions, depends on both the sequence and the metal ion concentration. How the latter influences the folding trajectories remains an important unsolved problem. Here, we examine th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8febdbbbe6f94d4bb7315713091a5182
https://hdl.handle.net/10356/86180
https://hdl.handle.net/10356/86180
Autor:
Anjum Ansari, Gerd Prehna, Ranjani Narayanan, Yogambigai Velmurugu, Li Zhu, Lisa J. Lapidus, Jorjethe Roca, Serguei V. Kuznetsov
Publikováno v:
Journal of the American Chemical Society. 134:18952-18963
We have investigated the multidimensionality of the free energy landscape accessible to a nucleic acid hairpin by measuring the relaxation kinetics in response to two very different perturbations of the folding/unfolding equilibrium, either a laser t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba5d6ed4fdafffcc39c1c4e069691b87
https://doi.org/10.1021/ja301218e
https://doi.org/10.1021/ja301218e
Autor:
Prasanth Narayanan, Jorjethe Roca, Anjum Ansari, Serguei Kouznetsov, Yogambigai Velmurugu, Ranjani Narayanan
Publikováno v:
Biophysical Journal. 108:236a
Pseudoknots are minimal tertiary motifs in RNA that are involved in many biological functions determined by their structure, stability and dynamics. They also stabilize the structures of several ribozymes and are often the rate-limiting step in their
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20cafbbbc9cba8c6b086424b9ce6c7bd
https://doi.org/10.1016/j.bpj.2014.11.1307
https://doi.org/10.1016/j.bpj.2014.11.1307