Active-Site Mutations of Diphtheria Toxin: Role of Tyrosine-65 in NAD Binding and ADP-Ribosylation

Biochemistry ◽  
1994 ◽  
Vol 33 (51) ◽  
pp. 15494-15500 ◽  
Author(s):  
Steven R. Blanke ◽  
Kathy Huang ◽  
R. John Collier
Keyword(s):  
Active Site ◽  
Diphtheria Toxin ◽  
Adp Ribosylation ◽  
Active Site Mutations

scholarly journals Active-site mutations of diphtheria toxin. Tryptophan 50 is a major determinant of NAD affinity.

1994 ◽  
Vol 269 (37) ◽  
pp. 23296-23301 ◽  
Author(s):  
B.A. Wilson ◽  
S.R. Blanke ◽  
K.A. Reich ◽  
R.J. Collier
Keyword(s):  
Active Site ◽  
Diphtheria Toxin ◽  
Major Determinant ◽  
Active Site Mutations

Active-site mutations of diphtheria toxin: effects of replacing glutamic acid-148 with aspartic acid, glutamine, or serine

Biochemistry ◽  
1990 ◽  
Vol 29 (37) ◽  
pp. 8643-8651 ◽  
Author(s):  
Brenda A. Wilson ◽  
Karl A. Reich ◽  
Beth R. Weinstein ◽  
R. John Collier
Keyword(s):  
Glutamic Acid ◽  
Aspartic Acid ◽  
Active Site ◽  
Diphtheria Toxin ◽  
Active Site Mutations

scholarly journals CD206+ macrophage is an accelerator of endometriotic-like lesion via promoting angiogenesis in the endometriosis mouse model

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Yosuke Ono ◽  
Osamu Yoshino ◽  
Takehiro Hiraoka ◽  
Erina Sato ◽  
Akiko Furue ◽  
...  
Keyword(s):  
Mouse Model ◽  
Diphtheria Toxin ◽  
Immunohistochemical Study ◽  
Mrna Levels ◽  
Cytokines And Chemokines ◽  
Diphtheria Toxin Receptor ◽  
Endothelial Cell Marker ◽  
Toxin Receptor ◽  
Group A

AbstractIn endometriosis, M2 MΦs are dominant in endometriotic lesions, but the actual role of M2 MΦ is unclear. CD206 positive (+) MΦ is classified in one of M2 type MΦs and are known to produce cytokines and chemokines. In the present study, we used CD206 diphtheria toxin receptor mice, which enable to deplete CD206+ cells with diphtheria toxin (DT) in an endometriosis mouse model. The depletion of CD206+ MΦ decreased the total weight of endometriotic-like lesions significantly (p < 0.05). In the endometriotic-like lesions in the DT group, a lower proliferation of endometriotic cells and the decrease of angiogenesis were observed. In the lesions, the mRNA levels of VEGFA and TGFβ1, angiogenic factors, in the DT group significantly decreased to approximately 50% and 30% of control, respectively. Immunohistochemical study revealed the expressions of VEGFA and an endothelial cell marker CD31 in lesions of the DT group, were dim compared to those in control. Also, the number of TGFβ1 expressing MΦ was significantly reduced compared to control. These data suggest that CD206+ MΦ promotes the formation of endometriotic-like lesions by inducing angiogenesis around the lesions.

scholarly journals HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Fa-Hui Sun ◽  
Peng Zhao ◽  
Nan Zhang ◽  
Lu-Lu Kong ◽  
Catherine C. L. Wong ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Active Site ◽  
Negative Charge ◽  
Structural Data ◽  
Dna Breaks ◽  
Adp Ribosylation ◽  
Local Conformation ◽  
Key Residues ◽  
Structural Insights

AbstractUpon binding to DNA breaks, poly(ADP-ribose) polymerase 1 (PARP1) ADP-ribosylates itself and other factors to initiate DNA repair. Serine is the major residue for ADP-ribosylation upon DNA damage, which strictly depends on HPF1. Here, we report the crystal structures of human HPF1/PARP1-CAT ΔHD complex at 1.98 Å resolution, and mouse and human HPF1 at 1.71 Å and 1.57 Å resolution, respectively. Our structures and mutagenesis data confirm that the structural insights obtained in a recent HPF1/PARP2 study by Suskiewicz et al. apply to PARP1. Moreover, we quantitatively characterize the key residues necessary for HPF1/PARP1 binding. Our data show that through salt-bridging to Glu284/Asp286, Arg239 positions Glu284 to catalyze serine ADP-ribosylation, maintains the local conformation of HPF1 to limit PARP1 automodification, and facilitates HPF1/PARP1 binding by neutralizing the negative charge of Glu284. These findings, along with the high-resolution structural data, may facilitate drug discovery targeting PARP1.

scholarly journals Role of Anions in Low pH-induced Translocation of Diphtheria Toxin

1989 ◽  
Vol 264 (19) ◽  
pp. 11367-11372 ◽  
Author(s):  
J Ø Moskaug ◽  
K Sandvig ◽  
S Olsnes
Keyword(s):  
Diphtheria Toxin ◽  
Low Ph
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