Transcription factor IIIA (TFIIIA) in the second decade

1996 ◽  
Vol 109 (3) ◽  
pp. 535-539 ◽  
Author(s):  
B.S. Shastry
Keyword(s):  
Transcription Factor ◽  
Amino Acid ◽  
Amino Acid Residue ◽  
Rna Binding ◽  
Current Knowledge ◽  
Zinc Fingers ◽  
Specific Factor ◽  
Transcription Factor Iiia ◽  
Dna And Rna

Transcription factor IIIA is a very extensively studied eukaryotic gene specific factor. It is a special member of the zinc finger family of nucleic acid binding proteins with multiple functions. Its N-terminal polypeptide (280 amino acid residue containing peptide; finger containing region) carries out sequence specific DNA and RNA binding and the C-terminal peptide (65 amino acid residue containing peptide; non-finger region) is involved in the transactivation process possibly by interacting with other general factors. It is a unique factor in the sense that it binds to two structurally different nucleic acids, DNA and RNA. It accomplishes this function through its zinc fingers, which are arranged into a cluster of nine motifs. Over the past three years there has been considerable interest in determining the structural features of zinc fingers, identifying the fingers that preferentially recognize DNA and RNA, defining the role of metal binding ligands and the linker region in promotor recognition and the role of C-terminal amino acid sequence in the gene activation. This article briefly reviews our current knowledge on this special protein in these areas.

scholarly journals The Unusual Role of Pro in Cu(II) Binding by His2-Cyclopentapeptide

2021 ◽  
Vol 22 (12) ◽  
pp. 6628
Author(s):  
Aleksandra Pieniężna ◽  
Aleksandra Kotynia ◽  
Justyna Brasuń
Keyword(s):  
Amino Acid ◽  
Potentiometric Titration ◽  
Amino Acid Residue ◽  
Strong Impact ◽  
Mononuclear Complexes ◽  
Study Results ◽  
Metal Ratio ◽  
Ph Range ◽  
L1 And L2

In this paper, we present findings from studying the interaction of copper(II) ions with the His2-cyclopentapeptide and the role of proline used for the purpose of potentiometric titration and UV-Vis, CD and EPR spectroscopic measurements. Experiments of two homodetic peptides differing by one amino acid residue were conducted for a ligand to metal ratio of 1:1 in the pH range 2.5–11.0. The presented studies reveal that peptides form only mononuclear complexes, and the CuH2L complex appears in the system first (for both L1 and L2). Study results show that the presence of Pro influences the structure of formed complexes and their stabilities and has a strong impact on the efficiency of copper(II) coordination.

Role of amino acid residue 90 in bioactivity and receptor binding capacity of tumor necrosis factor mutants

2007 ◽  
Vol 1774 (8) ◽  
pp. 1029-1035 ◽  
Author(s):  
Hiroko Shibata ◽  
Haruhiko Kamada ◽  
Kyoko Kobayashi-Nishibata ◽  
Yasuo Yoshioka ◽  
Toshihide Nishibata ◽  
...  
Keyword(s):  
Amino Acid ◽  
Tumor Necrosis Factor ◽  
Receptor Binding ◽  
Amino Acid Residue ◽  
Tumor Necrosis ◽  
Binding Capacity ◽  
Necrosis Factor

Role of Amino Acid Residue 187 of Poliovirus Polypeptide 2C in Determining the Guanidine Trait

Intervirology ◽  
1992 ◽  
Vol 33 (3) ◽  
pp. 165-172 ◽  
Author(s):  
Robert F. Baltera Jr. ◽  
Daniel R. Tershak
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue

Local stability identification and the role of a key aromatic amino acid residue in staphylococcal nuclease refolding

FEBS Journal ◽  
2005 ◽  
Vol 272 (15) ◽  
pp. 3960-3966 ◽  
Author(s):  
Zhengding Su ◽  
Jiun-Ming Wu ◽  
Huey-Jen Fang ◽  
Tian-Yow Tsong ◽  
Hueih-Min Chen
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Aromatic Amino Acid ◽  
Local Stability ◽  
Staphylococcal Nuclease ◽  
Aromatic Amino Acid Residue

scholarly journals RNA binding to human METTL3-METTL14 restricts N6-deoxyadenosine methylation of DNA in vitro

2022 ◽  
Author(s):  
Shan Qi ◽  
Javier Mota ◽  
Siu-Hong Chan ◽  
Johanna Villarreal ◽  
Nan Dai ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Rna Binding ◽  
Methyl Group ◽  
High Affinity ◽  
Methylation Of Dna ◽  
Dna And Rna ◽  
Close Proximity ◽  
Methylation Activity

Methyltransferase like-3 (METTL3) and METTL14 complex transfers a methyl group from S-adenosyl-L-methionine to N6 amino group of adenosine bases in RNA (m6A) and DNA (m6dA). Emerging evidence highlights a role of METTL3-METTL14 in the chromatin context, especially in processes where DNA and RNA are held in close proximity. However, a mechanistic framework about specificity for substrate RNA/DNA and their interrelationship remain unclear. By systematically studying methylation activity and binding affinity to a number of DNA and RNA oligos with different propensities to form inter- or intra-molecular duplexes or single-stranded molecules in vitro, we uncover an inverse relationship for substrate binding and methylation and show that METTL3-METTL14 preferentially catalyzes the formation of m6dA in single-stranded DNA (ssDNA), despite weaker binding affinity to DNA. In contrast, it binds structured RNAs with high affinity, but methylates the target adenosine in RNA (m6A) much less efficiently than it does in ssDNA. We also show that METTL3-METTL14-mediated methylation of DNA is largely restricted by structured RNA elements prevalent in long noncoding and other cellular RNAs.

scholarly journals POLIII-derived non-coding RNAs acting as scaffolds and decoys

2019 ◽  
Vol 11 (10) ◽  
pp. 880-885 ◽  
Author(s):  
Hendrik Täuber ◽  
Stefan Hüttelmaier ◽  
Marcel Köhn
Keyword(s):  
Rna Binding ◽  
Rna Binding Proteins ◽  
Current Knowledge ◽  
Cellular Functions ◽  
Control Of Gene Expression ◽  
Ribonucleoprotein Complexes ◽  
Small Ncrnas ◽  
Non Coding Rnas ◽  
And Function

Abstract A large variety of eukaryotic small structured POLIII-derived non-coding RNAs (ncRNAs) have been described in the past. However, for only few, e.g. 7SL and H1/MRP families, cellular functions are well understood. For the vast majority of these transcripts, cellular functions remain unknown. Recent findings on the role of Y RNAs and other POLIII-derived ncRNAs suggest an evolutionarily conserved function of these ncRNAs in the assembly and function of ribonucleoprotein complexes (RNPs). These RNPs provide cellular `machineries’, which are essential for guiding the fate and function of a variety of RNAs. In this review, we summarize current knowledge on the role of POLIII-derived ncRNAs in the assembly and function of RNPs. We propose that these ncRNAs serve as scaffolding factors that `chaperone’ RNA-binding proteins (RBPs) to form functional RNPs. In addition or associated with this role, some small ncRNAs act as molecular decoys impairing the RBP-guided control of RNA fate by competing with other RNA substrates. This suggests that POLIII-derived ncRNAs serve essential and conserved roles in the assembly of larger RNPs and thus the control of gene expression by indirectly guiding the fate of mRNAs and lncRNAs.

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