scholarly journals Correction: Synthetic approaches to nucleopeptides containing all four nucleobases, and nucleic acid-binding studies on a mixed-sequence nucleo-oligolysine

RSC Advances ◽  
2016 ◽  
Vol 6 (82) ◽  
pp. 78486-78486
Author(s):  
Giovanni N. Roviello ◽  
Domenica Musumeci

Correction for ‘Synthetic approaches to nucleopeptides containing all four nucleobases, and nucleic acid-binding studies on a mixed-sequence nucleo-oligolysine’ by Giovanni N. Roviello et al., RSC Adv., 2016, 6, 63578–63585.

RSC Advances ◽  
2016 ◽  
Vol 6 (68) ◽  
pp. 63578-63585 ◽  
Author(s):  
Giovanni N. Roviello ◽  
Domenica Musumeci

In this article we describe two solid-phase synthetic routes to obtain a nucleo-oligolysine α-peptide containing all four natural nucleobases.


2020 ◽  
Vol 48 (7) ◽  
pp. 3987-3997 ◽  
Author(s):  
Jillian Orans ◽  
Alexander R Kovach ◽  
Kirsten E Hoff ◽  
Nicola M Horstmann ◽  
Richard G Brennan

Abstract Hfq regulates bacterial gene expression post-transcriptionally by binding small RNAs and their target mRNAs, facilitating sRNA-mRNA annealing, typically resulting in translation inhibition and RNA turnover. Hfq is also found in the nucleoid and binds double-stranded (ds) DNA with a slight preference for A-tracts. Here, we present the crystal structure of the Escherichia coli Hfq Core bound to a 30 bp DNA, containing three 6 bp A-tracts. Although previously postulated to bind to the ‘distal’ face, three statistically disordered double stranded DNA molecules bind across the proximal face of the Hfq hexamer as parallel, straight rods with B-DNA like conformational properties. One DNA duplex spans the diameter of the hexamer and passes over the uridine-binding proximal-face pore, whereas the remaining DNA duplexes interact with the rims and serve as bridges between adjacent hexamers. Binding is sequence-independent with residues N13, R16, R17 and Q41 interacting exclusively with the DNA backbone. Atomic force microscopy data support the sequence-independent nature of the Hfq-DNA interaction and a role for Hfq in DNA compaction and nucleoid architecture. Our structure and nucleic acid-binding studies also provide insight into the mechanism of sequence-independent binding of Hfq to dsRNA stems, a function that is critical for proper riboregulation.


1993 ◽  
Vol 229 (1) ◽  
pp. 94-104 ◽  
Author(s):  
Andrej Surovoy ◽  
Jens Dannull ◽  
Karin Moelling ◽  
Gunther Jung

2003 ◽  
Vol 44 (8) ◽  
pp. 1663-1666 ◽  
Author(s):  
Tirayut Vilaivan ◽  
Chaturong Suparpprom ◽  
Preeyanut Duanglaor ◽  
Pongchai Harnyuttanakorn ◽  
Gordon Lowe

2018 ◽  
Vol 37 (10) ◽  
pp. 563-584 ◽  
Author(s):  
Mamta Tripathi ◽  
Chandra Gopal Giri ◽  
Devashish Das ◽  
Rama Pande ◽  
Sougata Sarkar ◽  
...  

2009 ◽  
Vol 6 (1) ◽  
pp. 199-205 ◽  
Author(s):  
Giovanni N. Roviello ◽  
Domenica Musumeci ◽  
Andrea De Cristofaro ◽  
Domenica Capasso ◽  
Sonia Di Gaetano ◽  
...  

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