Kinetic Analysis of the Interaction ofMos1Transposase with its Inverted Terminal Repeats Reveals New Insight into the Protein-DNA Complex Assembly

ChemBioChem ◽  
2014 ◽  
Vol 16 (1) ◽  
pp. 140-148
Author(s):  
Charles Esnault ◽  
Jérôme Jaillet ◽  
Nicolas Delorme ◽  
Nicolas Bouchet ◽  
Sylvaine Renault ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Complex Assembly ◽  
Inverted Terminal Repeats ◽  
Terminal Repeats ◽  
Dna Complex ◽  
Insight Into

Inverted terminal repeats in rabbit poxvirus and vaccinia virus DNA.

1978 ◽  
Vol 28 (1) ◽  
pp. 171-181 ◽  
Author(s):  
R Wittek ◽  
A Menna ◽  
H K Müller ◽  
D Schümperli ◽  
P G Boseley ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Inverted Terminal Repeats ◽  
Terminal Repeats

scholarly journals Molecular architecture of the endocytic TPLATE complex

2021 ◽  
Vol 7 (9) ◽  
pp. eabe7999
Author(s):  
Klaas Yperman ◽  
Jie Wang ◽  
Dominique Eeckhout ◽  
Joanna Winkler ◽  
Lam Dai Vu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Structural Approach ◽  
Eukaryotic Cells ◽  
Molecular Architecture ◽  
Membrane Proteome ◽  
Complex Assembly ◽  
Membrane Interaction ◽  
Structural Insight ◽  
Fresh Insight ◽  
Insight Into

Eukaryotic cells rely on endocytosis to regulate their plasma membrane proteome and lipidome. Most eukaryotic groups, except fungi and animals, have retained the evolutionary ancient TSET complex as an endocytic regulator. Unlike other coatomer complexes, structural insight into TSET is lacking. Here, we reveal the molecular architecture of plant TSET [TPLATE complex (TPC)] using an integrative structural approach. We identify crucial roles for specific TSET subunits in complex assembly and membrane interaction. Our data therefore generate fresh insight into the differences between the hexameric TSET in Dictyostelium and the octameric TPC in plants. Structural elucidation of this ancient adaptor complex represents the missing piece in the coatomer puzzle and vastly advances our functional as well as evolutionary insight into the process of endocytosis.

scholarly journals Sequences of Seven Complete Genomes of Human Parvovirus B19

2018 ◽  
Vol 7 (11) ◽  
Author(s):  
Yuhuan Qiu ◽  
Zehui Zhao ◽  
Jianming Qiu
Keyword(s):  
United States ◽  
Human Plasma ◽  
Parvovirus B19 ◽  
The United States ◽  
Human Parvovirus B19 ◽  
Genome Sequences ◽  
Complete Genomes ◽  
Inverted Terminal Repeats ◽  
Terminal Repeats

We are reporting the sequences of seven complete genomes of parvovirus B19, which were extracted from human plasma specimens collected in the United States. The seven B19 genome sequences, which are 5,596 nucleotides long and include the inverted terminal repeats (ITRs), share an identity of 96.73%.

Cryo-EM structure of the human cohesin-NIPBL-DNA complex

Science ◽  
2020 ◽  
Vol 368 (6498) ◽  
pp. 1454-1459 ◽  
Author(s):  
Zhubing Shi ◽  
Haishan Gao ◽  
Xiao-chen Bai ◽  
Hongtao Yu
Keyword(s):  
Electron Microscopy ◽  
Sister Chromatid ◽  
Base Pair ◽  
Adenosine Triphosphatase ◽  
Cryo Electron Microscopy ◽  
Synergistic Activation ◽  
Medium Resolution ◽  
Chromatid Cohesion ◽  
Dna Complex ◽  
Insight Into

As a ring-shaped adenosine triphosphatase (ATPase) machine, cohesin organizes the eukaryotic genome by extruding DNA loops and mediates sister chromatid cohesion by topologically entrapping DNA. How cohesin executes these fundamental DNA transactions is not understood. Using cryo–electron microscopy (cryo-EM), we determined the structure of human cohesin bound to its loader NIPBL and DNA at medium resolution. Cohesin and NIPBL interact extensively and together form a central tunnel to entrap a 72–base pair DNA. NIPBL and DNA promote the engagement of cohesin’s ATPase head domains and ATP binding. The hinge domains of cohesin adopt an “open washer” conformation and dock onto the STAG1 subunit. Our structure explains the synergistic activation of cohesin by NIPBL and DNA and provides insight into DNA entrapment by cohesin.

Modulation of RXR-DNA complex assembly by DNA context

2019 ◽  
Vol 481 ◽  
pp. 44-52 ◽  
Author(s):  
Judit Osz ◽  
Alastair G. McEwen ◽  
Justine Wolf ◽  
Pierre Poussin-Courmontagne ◽  
Carole Peluso-Iltis ◽  
...  
Keyword(s):  
Complex Assembly ◽  
Dna Context ◽  
Dna Complex

scholarly journals Structural insight into the ligand-receptor interaction between glycyrrhetinic acid (GA) and the high-mobility group protein B1 (HMGB1)-DNA complex

2012 ◽  
Vol 8 (23) ◽  
pp. 1147-1153 ◽  
Author(s):  
Hideaki Yamaguchi ◽  
◽  
Yumi Kidachi ◽  
Katsuyoshi Kamiie ◽  
Toshiro Noshita ◽  
...  
Keyword(s):  
High Mobility ◽  
Glycyrrhetinic Acid ◽  
High Mobility Group ◽  
Receptor Interaction ◽  
High Mobility Group Protein ◽  
Group Protein ◽  
Structural Insight ◽  
Dna Complex ◽  
Insight Into

scholarly journals Structure of the Tuberous Sclerosis Complex 2 (TSC2) N Terminus Provides Insight into Complex Assembly and Tuberous Sclerosis Pathogenesis

2016 ◽  
Vol 291 (38) ◽  
pp. 20008-20020 ◽  
Author(s):  
Reinhard Zech ◽  
Stephan Kiontke ◽  
Uwe Mueller ◽  
Andrea Oeckinghaus ◽  
Daniel Kümmel
Keyword(s):  
Tuberous Sclerosis ◽  
Tuberous Sclerosis Complex ◽  
Complex Assembly ◽  
N Terminus ◽  
Insight Into
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