scholarly journals A CRISPR RNA Is Closely Related With the Size of the Cascade Nucleoprotein Complex

2019 ◽  
Vol 10 ◽  
Author(s):  
Do-Heon Gu ◽  
Sung Chul Ha ◽  
Jeong-Sun Kim
Keyword(s):  
Nucleoprotein Complex

scholarly journals Interactions between Integrase and Excisionase in the Phage Lambda Excisive Nucleoprotein Complex

2002 ◽  
Vol 184 (18) ◽  
pp. 5200-5203 ◽  
Author(s):  
Eun Hee Cho ◽  
Richard I. Gumport ◽  
Jeffrey F. Gardner
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Mobility Shift ◽  
Host Chromosome ◽  
Amino Terminal ◽  
Nucleoprotein Complex ◽  
Carboxyl Terminal ◽  
Α Helix ◽  
Gel Mobility Shift ◽  
Amino Terminal Domain

ABSTRACT Bacteriophage lambda site-specific recombination comprises two overall reactions, integration into and excision from the host chromosome. Lambda integrase (Int) carries out both reactions. During excision, excisionase (Xis) helps Int to bind DNA and introduces a bend in the DNA that facilitates formation of the proper excisive nucleoprotein complex. The carboxyl-terminal α-helix of Xis is thought to interact with Int through direct protein-protein interactions. In this study, we used gel mobility shift assays to show that the amino-terminal domain of Int maintained cooperative interactions with Xis. This finding indicates that the amino-terminal arm-type DNA binding domain of Int interacts with Xis.

scholarly journals Nucleoprotein complex intermediates in HIV-1 integration

Methods ◽  
2009 ◽  
Vol 47 (4) ◽  
pp. 237-242 ◽  
Author(s):  
Min Li ◽  
Robert Craigie
Keyword(s):  
Nucleoprotein Complex ◽  
Hiv 1

An Iron–Copper–Nucleoprotein Complex in Animal Tissue

Nature ◽  
1941 ◽  
Vol 148 (3759) ◽  
pp. 595-596 ◽  
Author(s):  
K. C. SAHA ◽  
B. C. GUHA
Keyword(s):  
Animal Tissue ◽  
Iron Copper ◽  
Nucleoprotein Complex

scholarly journals Isolation and some properties of the nucleoprotein complex of Propionibacterium freudenreichii subsp.shermanii

1999 ◽  
Vol 79 (1) ◽  
pp. 187-196 ◽  
Author(s):  
Lena Vorobjeva ◽  
Aleksei Zinchenko ◽  
Evgeni Khodjaev ◽  
Galina Ponomareva ◽  
Elena Gordeeva
Keyword(s):  
Propionibacterium Freudenreichii ◽  
Nucleoprotein Complex

scholarly journals SlyA and H-NS Regulate Transcription of the Escherichia coli K5 Capsule Gene Cluster, and Expression of slyA in Escherichia coli Is Temperature-dependent, Positively Autoregulated, and Independent of H-NS

2007 ◽  
Vol 282 (46) ◽  
pp. 33326-33335 ◽  
Author(s):  
David Corbett ◽  
Hayley J. Bennett ◽  
Hamdia Askar ◽  
Jeffrey Green ◽  
Ian S. Roberts
Keyword(s):  
Escherichia Coli ◽  
Gene Cluster ◽  
Regulation Of Transcription ◽  
Temperature Dependent ◽  
Mobility Shift ◽  
E Coli ◽  
Dnase I Footprinting ◽  
Nucleoprotein Complex ◽  
Electrophoretic Mobility Shift Assays

In this paper, we present the first evidence of a role for the transcriptional regulator SlyA in the regulation of transcription of the Escherichia coli K5 capsule gene cluster and demonstrate, using a combination of reporter gene fusions, DNase I footprinting, and electrophoretic mobility shift assays, the dependence of transcription on the functional interplay between H-NS and SlyA. Both SlyA and H-NS bind to multiple overlapping sites within the promoter in vitro, but their binding is not mutually exclusive, resulting in a remodeled nucleoprotein complex. In addition, we show that expression of the E. coli slyA gene is temperature-regulated, positively autoregulated, and independent of H-NS.

scholarly journals The role of Cas8 in type I CRISPR interference

2015 ◽  
Vol 35 (3) ◽  
Author(s):  
Simon D.B. Cass ◽  
Karina A. Haas ◽  
Britta Stoll ◽  
Omer S. Alkhnbashi ◽  
Kundan Sharma ◽  
...  
Keyword(s):  
Nuclease Activity ◽  
Type I ◽  
Crispr Interference ◽  
Archaeal Species ◽  
Nucleoprotein Complex ◽  
Biochemical Analyses

We have used genetic and protein biochemical analyses in two archaeal species to identify that Cas8 is essential for CRISPR interference. We provide evidence that Cas8 functions as part of archaeal Cascade, an R-loop forming nucleoprotein complex, recognizing protospacer adjacent motifs (PAMs) on invader DNA. An RNA nuclease activity of Cas8 is also described.

scholarly journals The Unstructured N-terminal Tail of ParG Modulates Assembly of a Quaternary Nucleoprotein Complex in Transcription Repression

2005 ◽  
Vol 280 (31) ◽  
pp. 28683-28691 ◽  
Author(s):  
Emma Carmelo ◽  
Daniela Barillà ◽  
Alexander P. Golovanov ◽  
Lu-Yun Lian ◽  
Andrew Derome ◽  
...  
Keyword(s):  
Transcription Repression ◽  
Nucleoprotein Complex

Interaction of normal and mutant SRY proteins with DNA

1995 ◽  
Vol 350 (1333) ◽  
pp. 215-220 ◽  
Keyword(s):  
De Novo ◽  
Spatial Arrangement ◽  
Biochemical Properties ◽  
Chromatin Protein ◽  
Dna Structures ◽  
Testis Differentiation ◽  
Expression Of Genes ◽  
Target Sites ◽  
Nucleoprotein Complex ◽  
Complete Gonadal Dysgenesis

In mammals, sex determination is caused by the Y-chromosome gene SRY . The DNA-binding domain of human SRY protein is similar to those of the chromatin protein HMG1. Like HMG1, SRY binds to kinked DNA structures, and bends linear DNA sharply upon binding. We analysed the biochemical properties of mutant SRY proteins from five patients with complete gonadal dysgenesis: two bind and bend DNA almost normally, two bind inefficiently but bend DNA normally, and one binds DNA with almost normal affinity but produces a different angle. The mutations with moderate effect on complex formation can be transmitted to progeny, the ones with severe effects on either binding or bending are de novo . The angle induced by SRY depends on the exact DNA sequence, thus discriminating different target sites. We suggest that the exact spatial arrangement of the nucleoprotein complex organized by SRY in chromatin is essential for the expression of genes involved in testis differentiation.

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