scholarly journals Catalytic activity of human guanylate‐binding protein 1 coupled to the release of structural restraints imposed by the C‐terminal domain

FEBS Journal ◽  
2020 ◽  
Author(s):  
Semra Ince ◽  
Ping Zhang ◽  
Miriam Kutsch ◽  
Oktavian Krenczyk ◽  
Sergii Shydlovskyi ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Binding Protein ◽  
Terminal Domain ◽  
Structural Restraints ◽  
Guanylate Binding Protein

scholarly journals Healthy and preeclamptic pregnancies show differences in Guanylate-Binding Protein-1 plasma levels

2021 ◽  
Author(s):  
Joost H.N. Schuitemaker ◽  
Rik H.J. Beernink ◽  
Thomas I.F.H. Cremers ◽  
Sicco A. Scherjon ◽  
Maria G. Van Pampus ◽  
...  
Keyword(s):  
Plasma Levels ◽  
Binding Protein ◽  
Guanylate Binding Protein

scholarly journals Transient Kinetic Investigation of GTP Hydrolysis Catalyzed by Interferon-γ-induced hGBP1 (Human Guanylate Binding Protein 1)

2006 ◽  
Vol 281 (39) ◽  
pp. 28627-28635 ◽  
Author(s):  
Simone Kunzelmann ◽  
Gerrit J. K. Praefcke ◽  
Christian Herrmann
Keyword(s):  
Binding Protein ◽  
Interferon Γ ◽  
Kinetic Investigation ◽  
Gtp Hydrolysis ◽  
Guanylate Binding Protein

scholarly journals Identification of an N-terminal domain of eukaryotic DNA topoisomerase I dispensable for catalytic activity but essential for in vivo function.

1992 ◽  
Vol 267 (18) ◽  
pp. 12408-12411
Author(s):  
J Alsner ◽  
J.Q. Svejstrup ◽  
E Kjeldsen ◽  
B.S. Sørensen ◽  
O Westergaard
Keyword(s):  
Catalytic Activity ◽  
Topoisomerase I ◽  
Dna Topoisomerase I ◽  
Dna Topoisomerase ◽  
Terminal Domain ◽  
Eukaryotic Dna

scholarly journals Insight into the Dual Functions of Bacterial Enhancer-Binding Protein Rrp2 of Borrelia burgdorferi

2016 ◽  
Vol 198 (10) ◽  
pp. 1543-1552 ◽  
Author(s):  
Yanping Yin ◽  
Youyun Yang ◽  
Xuwu Xiang ◽  
Qian Wang ◽  
Zhang-Nv Yang ◽  
...  
Keyword(s):  
Dna Binding ◽  
Borrelia Burgdorferi ◽  
Binding Protein ◽  
Phosphorylation Site ◽  
Binding Motif ◽  
Cell Replication ◽  
Additional Function ◽  
Content Type ◽  
Terminal Domain ◽  
Enhancer Binding Protein

ABSTRACTIt is well established that the RpoN-RpoS sigma factor (σ54-σS) cascade plays an essential role in differential gene expression during the enzootic cycle ofBorrelia burgdorferi, the causative agent of Lyme disease. The RpoN-RpoS pathway is activated by the response regulator/σ54-dependent activator (also called bacterial enhancer-binding protein [bEBP]) Rrp2. One unique feature of Rrp2 is that this activator is essential for cell replication, whereas RpoN-RpoS is dispensable for bacterial growth. How Rrp2 controls cell replication, a function that is independent of RpoN-RpoS, remains to be elucidated. In this study, by generating a series of conditionalrrp2mutant strains, we demonstrated that the N-terminal receiver domain of Rrp2 is required for spirochetal growth. Furthermore, a D52A point mutation at the phosphorylation site within the N terminus of Rrp2 abolished cell replication. Mutation of the ATPase motif within the central domain of Rrp2 did not affect spirochetal replication, indicating that phosphorylation-dependent ATPase activity of Rrp2 for σ54activation is not required for cell growth. However, deletion of the C-terminal domain or a 16-amino-acid truncation of the helix-turn-helix (HTH) DNA-binding motif within the C-terminal domain of Rrp2 abolished spirochetal replication. It was shown that constitutive expression ofrpoSis deleterious to borrelial growth. We showed that the essential nature of Rrp2 is not due to an effect onrpoS. These data suggest that phosphorylation-dependent oligomerization and DNA binding of Rrp2 likely function as a repressor, independently of the activation of σ54, controlling an essential step of cell replication inB. burgdorferi.IMPORTANCEBacterial enhancer-binding proteins (bEBPs) are a unique group of transcriptional activators specifically required for σ54-dependent gene transcription. This work demonstrates that theB. burgdorferibEBP, Rrp2, has an additional function that is independent of σ54, that of its essentiality for spirochetal growth, and such a function is dependent on its N-terminal signal domain and C-terminal DNA-binding domain. These findings expand our knowledge on bEBP and provide a foundation to further study the underlying mechanism of this new function of bEBP.

Nonidentical Induction of the Guanylate Binding Protein and the 56K Protein by Type I and Type II Interferons

1986 ◽  
Vol 6 (4) ◽  
pp. 417-427 ◽  
Author(s):  
YIH-SHYUN E. CHENG ◽  
MARY F. BECKER-MANLEY ◽  
THAI D. NGUYEN ◽  
WILLIAM F. DEGRADO ◽  
GERALD J. JONAK
Keyword(s):  
Binding Protein ◽  
Type I ◽  
Type Ii ◽  
Guanylate Binding Protein

Evolution of the guanylate binding protein (GBP) genes: Emergence of GBP7 genes in primates and further acquisition of a unique GBP3 gene in simians

2021 ◽  
Vol 132 ◽  
pp. 79-81
Author(s):  
João Vasco Côrte-Real ◽  
Hanna-Mari Baldauf ◽  
Joana Abrantes ◽  
Pedro José Esteves
Keyword(s):  
Binding Protein ◽  
Guanylate Binding Protein

The N-terminal domain of the light-harvesting chlorophyll a/b -binding protein complex (LHCII) is essential for its acclimative proteolysis

FEBS Letters ◽  
2000 ◽  
Vol 466 (2-3) ◽  
pp. 385-388 ◽  
Author(s):  
Dan-Hui Yang ◽  
Harald Paulsen ◽  
Bertil Andersson
Keyword(s):  
Chlorophyll A ◽  
Protein Complex ◽  
Light Harvesting ◽  
Binding Protein ◽  
Terminal Domain

Identification of Guanylate-Binding Protein 1 as a Potential Oral Cancer Marker Involved in Cell Invasion Using Omics-Based Analysis

2011 ◽  
Vol 10 (8) ◽  
pp. 3778-3788 ◽  
Author(s):  
Chia-Jung Yu ◽  
Kai-Ping Chang ◽  
Yin-Ju Chang ◽  
Chia-Wei Hsu ◽  
Ying Liang ◽  
...  
Keyword(s):  
Oral Cancer ◽  
Cell Invasion ◽  
Binding Protein ◽  
Cancer Marker ◽  
Guanylate Binding Protein

Evaluation of Maltose Binding Protein-Tagged hATR Kinase Domain Catalytic Activity with p53 Ser-15 Phosphorylation

Biochemistry ◽  
2018 ◽  
Vol 57 (47) ◽  
pp. 6592-6603
Author(s):  
Rashmi Bhakuni ◽  
Althaf Shaik ◽  
Sivapriya Kirubakaran
Keyword(s):  
Catalytic Activity ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Kinase Domain

scholarly journals Identification of Rab6 as an N-ethylmaleimide-sensitive fusion protein-binding protein

2000 ◽  
Vol 352 (1) ◽  
pp. 165-173 ◽  
Author(s):  
Sang Yeul HAN ◽  
Dong Yoon PARK ◽  
Sang Dai PARK ◽  
Seung Hwan HONG
Keyword(s):  
Fusion Protein ◽  
Atpase Activity ◽  
Atp Hydrolysis ◽  
Polyclonal Antibodies ◽  
Binding Protein ◽  
Vesicular Transport ◽  
Brain Extract ◽  
Terminal Domain ◽  
Protein Receptor ◽  
And Function

In this study we show the interaction of N-ethylmaleimide-sensitive fusion protein (NSF) with a small GTP-binding protein, Rab6. NSF is an ATPase involved in the vesicular transport within eukaryotic cells. Using the yeast two-hybrid system, we have isolated new NSF-binding proteins from the rat lung cDNA library. One of them was Rab6, which is involved in the vesicular transport within the Golgi and trans-Golgi network as a Ras-like GTPase. We demonstrated that the N-terminal domain of NSF interacted with the C-terminal domain of Rab6, and these proteins were co-immunoprecipitated from the rat brain extract. This interaction was maintained preferentially in the presence of hydrolysable ATP. Recombinant NSF-His6 can also bind to C-terminal Rab6–glutathione S-transferase under the conditions to allow the ATP hydrolysis. Surprisingly, Rab6 stimulates the ATPase activity of NSF by approx. 2-fold as does α-soluble NSF attachment protein receptor. Anti-Rab6 polyclonal antibodies significantly inhibited the Rab6-stimulated ATPase activity of NSF. Furthermore, we found that Rab3 and Rab4 can also associate with NSF and stimulate its ATPase activity. Taken together, we propose a model in which Rab can form an ATP hydrolysis-regulated complex with NSF, and function as a signalling molecule to deliver the signal of vesicle fusion through the interaction with NSF.

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