scholarly journals 1P-102 Interaction between tetraplex structure of mouse telomeric DNA and telomeric DNA binding domains of mouse telomere binding protein Pot1(Nucleic acid:Interaction & Complex formation, The 47th Annual Meeting of the Biophysical Society of Japan)

2009 ◽  
Vol 49 (supplement) ◽  
pp. S79
Author(s):  
Kaoru Kaneda ◽  
Hidetaka Torigoe
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Annual Meeting ◽  
Binding Protein ◽  
Telomeric Dna ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Telomere Binding Protein ◽  
Biophysical Society

scholarly journals Cdc13 N-Terminal Dimerization, DNA Binding, and Telomere Length Regulation

2010 ◽  
Vol 30 (22) ◽  
pp. 5325-5334 ◽  
Author(s):  
Meghan T. Mitchell ◽  
Jasmine S. Smith ◽  
Mark Mason ◽  
Sandy Harper ◽  
David W. Speicher ◽  
...  
Keyword(s):  
Dna Binding ◽  
Telomere Length ◽  
Functional Characterization ◽  
Point Mutations ◽  
Telomeric Dna ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Length Regulation ◽  
Telomere Length Regulation

ABSTRACT The essential yeast protein Cdc13 facilitates chromosome end replication by recruiting telomerase to telomeres, and together with its interacting partners Stn1 and Ten1, it protects chromosome ends from nucleolytic attack, thus contributing to genome integrity. Although Cdc13 has been studied extensively, the precise role of its N-terminal domain (Cdc13N) in telomere length regulation remains unclear. Here we present a structural, biochemical, and functional characterization of Cdc13N. The structure reveals that this domain comprises an oligonucleotide/oligosaccharide binding (OB) fold and is involved in Cdc13 dimerization. Biochemical data show that Cdc13N weakly binds long, single-stranded, telomeric DNA in a fashion that is directly dependent on domain oligomerization. When introduced into full-length Cdc13 in vivo, point mutations that prevented Cdc13N dimerization or DNA binding caused telomere shortening or lengthening, respectively. The multiple DNA binding domains and dimeric nature of Cdc13 offer unique insights into how it coordinates the recruitment and regulation of telomerase access to the telomeres.

scholarly journals Effects of Complex Formation on Motion in DNA Binding Domains of ARFs

2019 ◽  
Vol 33 (S1) ◽  
Author(s):  
Natalie A George ◽  
Margaret C Carroll ◽  
Daniel Gonzalez ◽  
Jamie P Ellis
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Dna Binding Domains ◽  
Binding Domains
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