Proteins from Sulfolobus solfataricus (S. solfataricus), an extremophile, are active even at high temperatures. The single-stranded DNA (ssDNA) binding protein of S. solfataricus (SsoSSB) is overexpressed to protect ssDNA during DNA metabolism. Although SsoSSB has the potential to be applied in various areas, its structural and ssDNA binding properties at high temperatures have not been studied. We present the solution structure, backbone dynamics, and ssDNA binding properties of SsoSSB at 50...
[NMR paper] Characterization of an archaeal inorganic pyrophosphatase from Sulfolobus islandicus using a [(31)P]-NMR-based assay
Characterization of an archaeal inorganic pyrophosphatase from Sulfolobus islandicus using a -NMR-based assay
Inorganic pyrophosphatase catalyzes the conversion of pyrophosphate to phosphate and is often critical for driving reactions forward in cellular processes such as nucleic acid and protein synthesis. Commonly used methods for quantifying pyrophosphatase enzyme activity employ reacting liberated phosphate with a second molecule to produce absorbance changes or employing a second enzyme in coupled reactions to produce a product with a detectable absorbance. In this investigation, a...
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[NMR paper] NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs
NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs
The ribosomal S1 protein (rS1) is indispensable for translation initiation in Gram-negative bacteria. rS1 is a multidomain protein that acts as an RNA chaperone and ensures that mRNAs can bind the ribosome in a single-stranded conformation, which could be related to fast recognition. Although many ribosome structures were solved in recent years, a high-resolution structure of a two-domain mRNA-binding competent rS1 construct is not yet...
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07-08-2021 11:44 AM
[NMR paper] Expression, Purification, and Solution-State NMR Analysis of the Two Human Single-Stranded DNA-Binding Proteins hSSB1 (NABP2/OBFC2B) and hSSB2 (NAPB1/OBFC2A)
Expression, Purification, and Solution-State NMR Analysis of the Two Human Single-Stranded DNA-Binding Proteins hSSB1 (NABP2/OBFC2B) and hSSB2 (NAPB1/OBFC2A)
Single-stranded DNA-binding proteins (SSBs) are essential to all living organisms as protectors and guardians of the genome. Apart from the well-characterized RPA, humans have also evolved two further SSBs, termed hSSB1 and hSSB2. Over the last few years, we have used NMR spectroscopy to determine the molecular and structural details of both hSSBs and their interactions with DNA and RNA. Here we provide a detailed overview of how to...
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Replication Protein A Prohibits Diffusion of the PCNASliding Clamp along Single-Stranded DNA
Replication Protein A Prohibits Diffusion of the PCNASliding Clamp along Single-Stranded DNA
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01213/20170223/images/medium/bi-2016-01213e_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01213
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/acrZkrDOr0Q
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03-01-2017 04:13 AM
[NMR paper] Screening protein - single stranded RNA complexes by NMR spectroscopy for structure determination.
Screening protein - single stranded RNA complexes by NMR spectroscopy for structure determination.
Screening protein - single stranded RNA complexes by NMR spectroscopy for structure determination.
Methods. 2013 Oct 1;
Authors: Foot JN, Feracci M, Dominguez C
Abstract
In the past few years, RNA molecules have been revealed to be at the center of numerous biological processes. Long considered as passive molecules transferring genetic information from DNA to proteins, it is now well established that RNA molecules play important regulatory...
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10-08-2013 02:04 PM
Screening protein – single stranded RNA complexes by NMR spectroscopy for structure determination
Screening protein – single stranded RNA complexes by NMR spectroscopy for structure determination
Publication date: Available online 1 October 2013
Source:Methods</br>
Author(s): Jaelle N. Foot , Mikael Feracci , Cyril Dominguez</br>
In the past few years, RNA molecules have been revealed to be at the center of numerous biological processes. Long considered as passive molecules transferring genetic information from DNA to proteins, it is now well established that RNA molecules play important regulatory roles. Associated with that, the number of identified RNA...
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10-01-2013 11:15 PM
[NMR paper] Secondary structure of the single-stranded DNA binding protein encoded by filamentous
Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
Eur J Biochem. 1994 Sep 1;224(2):663-76
Authors: Folmer RH, Folkers PJ, Kaan A, Jonker AJ, Aelen JM, Konings RN, Hilbers CW
Nuclear magnetic resonance...
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[NMR paper] Identification of the single-stranded DNA binding surface of the transcriptional coac
Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
J Biol Chem. 1999 Feb 5;274(6):3693-9
Authors: Werten S, Wechselberger R, Boelens R, van der Vliet PC, Kaptein R
The C-terminal domain of the eukaryotic transcriptional cofactor PC4...