scholarly journals Critical Role of N and C Terminal Domains of Bacteriophage T4 Single-Stranded Binding Protein (GP32) in Transient Binding Conformations and Reorganization Measured using Force Spectroscopy

2021 ◽  
Vol 120 (3) ◽  
pp. 35a-36a
Author(s):  
Benjamin Cashen ◽  
Michael Morse ◽  
Richard L. Karpel ◽  
Ioulia F. Rouzina ◽  
Mark C. Williams
FEBS Open Bio ◽  
2018 ◽  
Vol 8 (12) ◽  
pp. 1964-1976 ◽  
Author(s):  
Nirmala Tilija Pun ◽  
Amrita Khakurel ◽  
Aastha Shrestha ◽  
Sang‐Hyun Kim ◽  
Pil‐Hoon Park

2001 ◽  
Vol 167 (5) ◽  
pp. 2759-2765 ◽  
Author(s):  
Didier Le Roy ◽  
Franco Di Padova ◽  
Yoshiyuki Adachi ◽  
Michel Pierre Glauser ◽  
Thierry Calandra ◽  
...  

Blood ◽  
2007 ◽  
Vol 110 (7) ◽  
pp. 2390-2398 ◽  
Author(s):  
Rigu Gupta ◽  
Sudha Sharma ◽  
Joshua A. Sommers ◽  
Mark K. Kenny ◽  
Sharon B. Cantor ◽  
...  

The BRCA1 associated C-terminal helicase (BACH1, designated FANCJ) is implicated in the chromosomal instability genetic disorder Fanconi anemia (FA) and hereditary breast cancer. A critical role of FANCJ helicase may be to restart replication as a component of downstream events that occur during the repair of DNA cross-links or double-strand breaks. We investigated the potential interaction of FANCJ with replication protein A (RPA), a single-stranded DNA-binding protein implicated in both DNA replication and repair. FANCJ and RPA were shown to coimmunoprecipitate most likely through a direct interaction of FANCJ and the RPA70 subunit. Moreover, dependent on the presence of BRCA1, FANCJ colocalizes with RPA in nuclear foci after DNA damage. Our data are consistent with a model in which FANCJ associates with RPA in a DNA damage-inducible manner and through the protein interaction RPA stimulates FANCJ helicase to better unwind duplex DNA substrates. These findings identify RPA as the first regulatory partner of FANCJ. The FANCJ-RPA interaction is likely to be important for the role of the helicase to more efficiently unwind DNA repair intermediates to maintain genomic stability.


2001 ◽  
Vol 359 (2) ◽  
pp. 255 ◽  
Author(s):  
Patrick PROVOST ◽  
Johanne DOUCET ◽  
Alexander STOCK ◽  
Günther GERISCH ◽  
Bengt SAMUELSSON ◽  
...  

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e79386 ◽  
Author(s):  
Mas Rizky A. A. Syamsunarno ◽  
Tatsuya Iso ◽  
Hirofumi Hanaoka ◽  
Aiko Yamaguchi ◽  
Masaru Obokata ◽  
...  

Genes ◽  
2019 ◽  
Vol 10 (11) ◽  
pp. 941 ◽  
Author(s):  
Izabella Bajusz ◽  
Surya Henry ◽  
Enikő Sutus ◽  
Gergő Kovács ◽  
Melinda K. Pirity

Separation of germline cells from somatic lineages is one of the earliest decisions of embryogenesis. Genes expressed in germline cells include apoptotic and meiotic factors, which are not transcribed in the soma normally, but a number of testis-specific genes are active in numerous cancer types. During germ cell development, germ-cell-specific genes can be regulated by specific transcription factors, retinoic acid signaling and multimeric protein complexes. Non-canonical polycomb repressive complexes, like ncPRC1.6, play a critical role in the regulation of the activity of germ-cell-specific genes. RING1 and YY1 binding protein (RYBP) is one of the core members of the ncPRC1.6. Surprisingly, the role of Rybp in germ cell differentiation has not been defined yet. This review is focusing on the possible role of Rybp in this process. By analyzing whole-genome transcriptome alterations of the Rybp-/- embryonic stem (ES) cells and correlating this data with experimentally identified binding sites of ncPRC1.6 subunits and retinoic acid receptors in ES cells, we propose a model how germ-cell-specific transcription can be governed by an RYBP centered regulatory network, underlining the possible role of RYBP in germ cell differentiation and tumorigenesis.


2006 ◽  
Vol 177 (9) ◽  
pp. 6308-6316 ◽  
Author(s):  
Viviana P. Ferreira ◽  
Andrew P. Herbert ◽  
Henry G. Hocking ◽  
Paul N. Barlow ◽  
Michael K. Pangburn

2014 ◽  
Vol 10 (5) ◽  
pp. 2306-2312 ◽  
Author(s):  
KA-PUI LEUNG ◽  
YI-HONG QU ◽  
DONG-FANG QIAO ◽  
WEI-BING XIE ◽  
DONG-RI LI ◽  
...  

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