Structure of a Tethered Cationic 3-Aminopropyl Chain Incorporated into an Oligodeoxynucleotide:  Evidence for 3‘-Orientation in the Major Groove Accompanied by DNA Bending

2002 ◽  
Vol 124 (29) ◽  
pp. 8553-8560 ◽  
Author(s):  
Zhijun Li ◽  
Li Huang ◽  
Prasad Dande ◽  
Barry Gold ◽  
Michael P. Stone
Keyword(s):  
Dna Bending ◽  
Major Groove

scholarly journals Selective DNA bending by a variety of bZIP proteins.

1993 ◽  
Vol 13 (9) ◽  
pp. 5479-5489 ◽  
Author(s):  
T K Kerppola ◽  
T Curran
Keyword(s):  
Dna Bending ◽  
Major Groove ◽  
Bent Dna ◽  
Dna Structures ◽  
Protein Dimers ◽  
Bzip Proteins ◽  
Related Proteins ◽  
Combinatorial Interactions ◽  
Bend Angles ◽  
Bzip Family

We have investigated DNA bending by bZIP family proteins that can bind to the AP-1 site. DNA bending is widespread, although not universal, among members of this family. Different bZIP protein dimers induced distinct DNA bends. The DNA bend angles ranged from virtually 0 to greater than 40 degrees as measured by phasing analysis and were oriented toward both the major and the minor grooves at the center of the AP-1 site. The DNA bends induced by the various heterodimeric complexes suggested that each component of the complex induced an independent DNA bend as previously shown for Fos and Jun. The Fos-related proteins Fra1 and Fra2 bent DNA in the same orientation as Fos but induced smaller DNA bend angles. ATF2 also bent DNA toward the minor groove in heterodimers formed with Fos, Fra2, and Jun. CREB and ATF1, which favor binding to the CRE site, did not induce significant DNA bending. Zta, which is a divergent member of the bZIP family, bent DNA toward the major groove. A variety of DNA structures can therefore be induced at the AP-1 site through combinatorial interactions between different bZIP family proteins. This diversity of DNA structures may contribute to regulatory specificity among the plethora of proteins that can bind to the AP-1 site.

scholarly journals Selective DNA bending by a variety of bZIP proteins

1993 ◽  
Vol 13 (9) ◽  
pp. 5479-5489
Author(s):  
T K Kerppola ◽  
T Curran
Keyword(s):  
Dna Bending ◽  
Major Groove ◽  
Bent Dna ◽  
Dna Structures ◽  
Protein Dimers ◽  
Bzip Proteins ◽  
Related Proteins ◽  
Combinatorial Interactions ◽  
Bend Angles ◽  
Bzip Family

We have investigated DNA bending by bZIP family proteins that can bind to the AP-1 site. DNA bending is widespread, although not universal, among members of this family. Different bZIP protein dimers induced distinct DNA bends. The DNA bend angles ranged from virtually 0 to greater than 40 degrees as measured by phasing analysis and were oriented toward both the major and the minor grooves at the center of the AP-1 site. The DNA bends induced by the various heterodimeric complexes suggested that each component of the complex induced an independent DNA bend as previously shown for Fos and Jun. The Fos-related proteins Fra1 and Fra2 bent DNA in the same orientation as Fos but induced smaller DNA bend angles. ATF2 also bent DNA toward the minor groove in heterodimers formed with Fos, Fra2, and Jun. CREB and ATF1, which favor binding to the CRE site, did not induce significant DNA bending. Zta, which is a divergent member of the bZIP family, bent DNA toward the major groove. A variety of DNA structures can therefore be induced at the AP-1 site through combinatorial interactions between different bZIP family proteins. This diversity of DNA structures may contribute to regulatory specificity among the plethora of proteins that can bind to the AP-1 site.

Bis(dipyridophenazine)copper(ii) complex as major groove directing synthetic hydrolase

2004 ◽  
pp. 1896 ◽  
Author(s):  
Tarkeshwar Gupta ◽  
Shanta Dhar ◽  
Munirathinam Nethaji ◽  
Akhil R. Chakravarty
Keyword(s):  
Major Groove

scholarly journals Kaposi's Sarcoma-Associated Herpesvirus Latency-Associated Nuclear Antigen Induces a Strong Bend on Binding to Terminal Repeat DNA

2005 ◽  
Vol 79 (21) ◽  
pp. 13829-13836 ◽  
Author(s):  
Lai-Yee Wong ◽  
Angus C. Wilson
Keyword(s):  
Dna Replication ◽  
Kaposi's Sarcoma ◽  
Kaposi’S Sarcoma ◽  
Nuclear Antigen ◽  
Major Groove ◽  
Repeat Dna ◽  
Initiation Of Dna Replication ◽  
Kaposi's Sarcoma Associated Herpesvirus ◽  
Kaposi’S Sarcoma Associated Herpesvirus ◽  
Herpesvirus Genome

ABSTRACT During latency, the Kaposi's sarcoma-associated herpesvirus genome is maintained as a circular episome, replicating in synchrony with host chromosomes. Replication requires the latency-associated nuclear antigen (LANA) and an origin of latent DNA replication located in the viral terminal repeats, consisting of two LANA binding sites (LBSs) and a GC-rich sequence. Here, we show that the recruitment of a LANA dimer to high-affinity site LBS-1 bends DNA by 57° and towards the major groove. The cooccupancy of LBS-1 and lower-affinity LBS-2 induces a symmetrical bend of 110°. By changing the origin architecture, LANA may help to assemble a specific nucleoprotein structure important for the initiation of DNA replication.

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