Novel zinc finger motif in the basal transcriptional machinery: Three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS

Biochemistry ◽  
1993 ◽  
Vol 32 (38) ◽  
pp. 9944-9959 ◽  
Author(s):  
Xiuqi Qian ◽  
Shai N. Gozani ◽  
HoSup Yoon ◽  
ChoonJu Jeon ◽  
Kan Agarwal ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Zinc Finger ◽  
Three Dimensional ◽  
Elongation Factor ◽  
Binding Domain ◽  
Transcriptional Elongation ◽  
Zinc Finger Motif ◽  
Nucleic Acid Binding ◽  
Nmr Studies ◽  
Basal Transcriptional Machinery

scholarly journals Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS

Nature ◽  
1993 ◽  
Vol 365 (6443) ◽  
pp. 277-279 ◽  
Author(s):  
Xiuqu Qian ◽  
ChoonJu Jeon ◽  
HoSup Yoon ◽  
Kan Agarwal ◽  
Michael A. Weiss
Keyword(s):  
Nucleic Acid ◽  
Elongation Factor ◽  
Binding Motif ◽  
Transcriptional Elongation ◽  
Nucleic Acid Binding

scholarly journals Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS

Nature ◽  
1995 ◽  
Vol 376 (6537) ◽  
pp. 279-279 ◽  
Author(s):  
Xiuqu Qian ◽  
ChoonJu Jeon ◽  
HoSup Yoon ◽  
Kan Agarwal ◽  
Michael A. Weiss
Keyword(s):  
Nucleic Acid ◽  
Elongation Factor ◽  
Binding Motif ◽  
Transcriptional Elongation ◽  
Nucleic Acid Binding

scholarly journals Identification of a Nucleic Acid Binding Domain in Eukaryotic Initiation Factor eIFiso4G from Wheat

1999 ◽  
Vol 274 (15) ◽  
pp. 10603-10608 ◽  
Author(s):  
Chang-Yub Kim ◽  
Katsuyuki Takahashi ◽  
Tran B. Nguyen ◽  
Justin K. M. Roberts ◽  
Cecelia Webster
Keyword(s):  
Nucleic Acid ◽  
Binding Domain ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Nucleic Acid Binding

Crystal structure of the hinge domain of Smchd1 reveals its dimerization mode and nucleic acid–binding residues

2020 ◽  
Vol 13 (636) ◽  
pp. eaaz5599 ◽  
Author(s):  
Kelan Chen ◽  
Richard W. Birkinshaw ◽  
Alexandra D. Gurzau ◽  
Iromi Wanigasuriya ◽  
Ruoyun Wang ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Muscular Dystrophy ◽  
Three Dimensional ◽  
Underlying Mechanism ◽  
Structural Features ◽  
Facioscapulohumeral Muscular Dystrophy ◽  
Dimensional Structure ◽  
Nucleic Acid Binding ◽  
X Ray Crystallography ◽  
Hinge Domain

Structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) is an epigenetic regulator in which polymorphisms cause the human developmental disorder, Bosma arhinia micropthalmia syndrome, and the degenerative disease, facioscapulohumeral muscular dystrophy. SMCHD1 is considered a noncanonical SMC family member because its hinge domain is C-terminal, because it homodimerizes rather than heterodimerizes, and because SMCHD1 contains a GHKL-type, rather than an ABC-type ATPase domain at its N terminus. The hinge domain has been previously implicated in chromatin association; however, the underlying mechanism involved and the basis for SMCHD1 homodimerization are unclear. Here, we used x-ray crystallography to solve the three-dimensional structure of the Smchd1 hinge domain. Together with structure-guided mutagenesis, we defined structural features of the hinge domain that participated in homodimerization and nucleic acid binding, and we identified a functional hotspot required for chromatin localization in cells. This structure provides a template for interpreting the mechanism by which patient polymorphisms within the SMCHD1 hinge domain could compromise function and lead to facioscapulohumeral muscular dystrophy.

Cloning of the nucleic acid-binding domain of the rat HnRNP C-type protein

1990 ◽  
Vol 1048 (2-3) ◽  
pp. 306-309 ◽  
Author(s):  
Z.Dave Sharp ◽  
Kelly P. Smith ◽  
Zhaodan Cao ◽  
Sharon Helsel
Keyword(s):  
Nucleic Acid ◽  
Binding Domain ◽  
Nucleic Acid Binding ◽  
Type Protein ◽  
Hnrnp C

scholarly journals Structure and nucleic acid binding properties of KOW domains 4 and 6–7 of human transcription elongation factor DSIF

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Philipp K. Zuber ◽  
Lukas Hahn ◽  
Anne Reinl ◽  
Kristian Schweimer ◽  
Stefan H. Knauer ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Transcription Elongation ◽  
Elongation Factor ◽  
Nucleic Acid Binding ◽  
Binding Properties ◽  
Transcription Elongation Factor

scholarly journals Nucleic-acid-binding properties of the C2-L1Tc nucleic acid chaperone encoded by L1Tc retrotransposon

2009 ◽  
Vol 424 (3) ◽  
pp. 479-490 ◽  
Author(s):  
Sara R. Heras ◽  
M. Carmen Thomas ◽  
Francisco Macias ◽  
Manuel E. Patarroyo ◽  
Carlos Alonso ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Zinc Finger ◽  
Rna Binding ◽  
Nuclear Localization Sequence ◽  
Nucleic Acid Binding ◽  
Binding Model ◽  
Nucleic Acid Chaperone ◽  
Localization Sequence ◽  
Cysteine Motifs

It has been reported previously that the C2-L1Tc protein located in the Trypanosoma cruzi LINE (long interspersed nuclear element) L1Tc 3′ terminal end has NAC (nucleic acid chaperone) activity, an essential activity for retrotransposition of LINE-1. The C2-L1Tc protein contains two cysteine motifs of a C2H2 type, similar to those present in TFIIIA (transcription factor IIIA). The cysteine motifs are flanked by positively charged amino acid regions. The results of the present study show that the C2-L1Tc recombinant protein has at least a 16-fold higher affinity for single-stranded than for double-stranded nucleic acids, and that it exhibits a clear preference for RNA binding over DNA. The C2-L1Tc binding profile (to RNA and DNA) corresponds to a non-co-operative-binding model. The zinc fingers present in C2-L1Tc have a different binding affinity to nucleic acid molecules and also different NAC activity. The RRR and RRRKEK [NLS (nuclear localization sequence)] sequences, as well as the C2H2 zinc finger located immediately downstream of these basic stretches are the main motifs responsible for the strong affinity of C2-L1Tc to RNA. These domains also contribute to bind single- and double-stranded DNA and have a duplex-stabilizing effect. However, the peptide containing the zinc finger situated towards the C-terminal end of C2-L1Tc protein has a slight destabilization effect on a mismatched DNA duplex and shows a strong preference for single-stranded nucleic acids, such as C2-L1Tc. These results provide further insight into the essential properties of the C2-L1Tc protein as a NAC.

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