Role of Ionizing Amino Acid Residues in the Process of DNA Binding by Human AP Endonuclease 1 and in Its Catalysis

2019 ◽  
Vol 123 (45) ◽  
pp. 9546-9556 ◽  
Author(s):  
Irina V. Alekseeva ◽  
Artemiy S. Bakman ◽  
Yury N. Vorobjev ◽  
Olga S. Fedorova ◽  
Nikita A. Kuznetsov
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Amino Acid Residues ◽  
Ap Endonuclease ◽  
Ap Endonuclease 1

3‘-5‘ Exonuclease of Klenow Fragment:  Role of Amino Acid Residues within the Single-Stranded DNA Binding Region in Exonucleolysis and Duplex DNA Melting†

Biochemistry ◽  
2002 ◽  
Vol 41 (12) ◽  
pp. 3943-3951 ◽  
Author(s):  
Wai-Chung Lam ◽  
Elizabeth H. Z. Thompson ◽  
Olga Potapova ◽  
Xiaojun Chen Sun ◽  
Catherine M. Joyce ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Dna Melting ◽  
Duplex Dna ◽  
Amino Acid Residues ◽  
Klenow Fragment ◽  
Binding Region ◽  
Single Stranded Dna

scholarly journals Structural comparison of AP endonucleases from the exonuclease III family reveals new amino acid residues in human AP endonuclease 1 that are involved in incision of damaged DNA

Biochimie ◽  
2016 ◽  
Vol 128-129 ◽  
pp. 20-33 ◽  
Author(s):  
Modesto Redrejo-Rodríguez ◽  
Armelle Vigouroux ◽  
Aibek Mursalimov ◽  
Inga Grin ◽  
Doria Alili ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Structural Comparison ◽  
Ap Endonuclease ◽  
Exonuclease Iii ◽  
Ap Endonuclease 1 ◽  
Damaged Dna

Role of Specific Amino Acid Residues in T4 Endonuclease V That Alter Nontarget DNA Binding†

Biochemistry ◽  
1997 ◽  
Vol 36 (14) ◽  
pp. 4080-4088 ◽  
Author(s):  
Simon G. Nyaga ◽  
M. L. Dodson ◽  
R. Stephen Lloyd
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Amino Acid Residues ◽  
Specific Amino Acid ◽  
Endonuclease V

scholarly journals Deletion of the Actin-Associated Tropomyosin Tpm3 Leads to Reduced Cell Complexity in Cultured Hippocampal Neurons—New Insights into the Role of the C-Terminal Region of Tpm3.1

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 715
Author(s):  
Tamara Tomanić ◽  
Claire Martin ◽  
Holly Stefen ◽  
Esmeralda Parić ◽  
Peter Gunning ◽  
...  
Keyword(s):  
Amino Acid ◽  
Hippocampal Neurons ◽  
Molecular Mechanisms ◽  
Growth Cones ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
C Terminus ◽  
Primary Mouse ◽  
Terminal Amino

Tropomyosins (Tpms) have been described as master regulators of actin, with Tpm3 products shown to be involved in early developmental processes, and the Tpm3 isoform Tpm3.1 controlling changes in the size of neuronal growth cones and neurite growth. Here, we used primary mouse hippocampal neurons of C57/Bl6 wild type and Bl6Tpm3flox transgenic mice to carry out morphometric analyses in response to the absence of Tpm3 products, as well as to investigate the effect of C-terminal truncation on the ability of Tpm3.1 to modulate neuronal morphogenesis. We found that the knock-out of Tpm3 leads to decreased neurite length and complexity, and that the deletion of two amino acid residues at the C-terminus of Tpm3.1 leads to more detrimental changes in neurite morphology than the deletion of six amino acid residues. We also found that Tpm3.1 that lacks the 6 C-terminal amino acid residues does not associate with stress fibres, does not segregate to the tips of neurites, and does not impact the amount of the filamentous actin pool at the axonal growth cones, as opposed to Tpm3.1, which lacks the two C-terminal amino acid residues. Our study provides further insight into the role of both Tpm3 products and the C-terminus of Tpm3.1, and it forms the basis for future studies that aim to identify the molecular mechanisms underlying Tpm3.1 targeting to different subcellular compartments.

scholarly journals Amino Acid Residues in Both the Protein Splicing and Endonuclease Domains of the PI-SceI Intein Mediate DNA Binding

1998 ◽  
Vol 273 (8) ◽  
pp. 4607-4615 ◽  
Author(s):  
Zening He ◽  
Michael Crist ◽  
Hsiao-ching Yen ◽  
Xiaoqun Duan ◽  
Florante A. Quiocho ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Protein Splicing ◽  
Amino Acid Residues

scholarly journals Filamin A-Bound PEBP2β/CBFβ Is Retained in the Cytoplasm and Prevented from Functioning as a Partner of the Runx1 Transcription Factor

2005 ◽  
Vol 25 (3) ◽  
pp. 1003-1012 ◽  
Author(s):  
Naomi Yoshida ◽  
Takehiro Ogata ◽  
Kenji Tanabe ◽  
Songhua Li ◽  
Megumi Nakazato ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Amino Acid ◽  
Dna Binding ◽  
Binding Domain ◽  
Actin Binding ◽  
Regulatory Domain ◽  
Amino Acid Residues ◽  
Filamin A ◽  
Actin Binding Protein ◽  
Binding Subunit

ABSTRACT The heterodimeric transcription factor PEBP2/CBF is composed of a DNA-binding subunit, called Runx1, and a non-DNA-binding subunit, called PEBP2β/CBFβ. The Runx1 protein is detected exclusively in the nuclei of most cells and tissues, whereas PEBP2β is located in the cytoplasm. We addressed the mechanism by which PEBP2β localizes to the cytoplasm and found that it is associated with filamin A, an actin-binding protein. Filamin A retains PEBP2β in the cytoplasm, thereby hindering its engagement as a Runx1 partner. The interaction with filamin A is mediated by a region within PEBP2β that includes amino acid residues 68 to 93. The deletion of this region or the repression of filamin A enables PEBP2β to translocate to the nucleus. Based on these observations, we propose that PEBP2β has two distinct domains, a newly defined regulatory domain that interacts with filamin A and the previously identified Runx1-binding domain.

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