An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of .lambda. repressor

Biochemistry ◽  
1986 ◽  
Vol 25 (20) ◽  
pp. 5992-5998 ◽  
Author(s):  
R. T. Sauer ◽  
K. Hehir ◽  
R. S. Stearman ◽  
M. A. Weiss ◽  
A. Jeitler-Nilsson ◽  
...  
Keyword(s):  
Dna Binding ◽  
Lambda Repressor ◽  
Terminal Domain ◽  
The Stability

scholarly journals Role of the N-terminal domain of the human DMC1 protein in octamer formation and DNA binding. VOLUME 280 (2005) PAGES 28382-28387

2006 ◽  
Vol 281 (50) ◽  
pp. 38966
Author(s):  
Takashi Kinebuchi ◽  
Wataru Kagawa ◽  
Hitoshi Kurumizaka ◽  
Shigeyuki Yokoyama
Keyword(s):  
Dna Binding ◽  
Terminal Domain

The Stability Enhancement of Nitrile Hydratase from Bordetella petrii by Swapping the C-terminal Domain of β subunit

2015 ◽  
Vol 178 (8) ◽  
pp. 1481-1487 ◽  
Author(s):  
Weifeng Sun ◽  
Longbao Zhu ◽  
Xianggui Chen ◽  
Lunjie Wu ◽  
Zhemin Zhou ◽  
...  
Keyword(s):  
Nitrile Hydratase ◽  
Β Subunit ◽  
Terminal Domain ◽  
The Stability ◽  
Stability Enhancement

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.

scholarly journals DNA-binding Activity of the ERp57 C-terminal Domain Is Related to a Redox-dependent Conformational Change

2007 ◽  
Vol 282 (14) ◽  
pp. 10299-10310 ◽  
Author(s):  
Caterina Grillo ◽  
Chiara D'Ambrosio ◽  
Valerio Consalvi ◽  
Roberta Chiaraluce ◽  
Andrea Scaloni ◽  
...  
Keyword(s):  
Dna Binding ◽  
Conformational Change ◽  
Binding Activity ◽  
Terminal Domain ◽  
Dna Binding Activity

Abstract 42: Differential Contribution Of The N- And C-terminal Domains To The Folding And Function Of Tandem Calponin-homology Domains

2014 ◽  
Vol 115 (suppl_1) ◽  
Author(s):  
Krishna Mallela ◽  
Swati Bandi ◽  
Surinder Singh ◽  
Geoffrey Armstrong
Keyword(s):  
Full Length ◽  
Actin Binding ◽  
Main Function ◽  
Calponin Homology ◽  
Terminal Domain ◽  
Binding Domains ◽  
Binding Function ◽  
Ch2 Domain ◽  
The Stability ◽  
And Function

Tandem calponin-homology (CH) domains constitute a major class of actin-binding domains that include dystrophin and utrophin, the two key proteins involved in muscular dystrophy. Despite their importance, how their structure controls their function is not understood. Here, we study the contribution of individual CH domains to the actin-binding function and thermodynamic stability of utrophin’s tandem CH domain. Traditional actin co-sedimentation assays indicate that the isolated C-terminal CH2 domain binds weakly to F-actin when compared with the full-length tandem CH domain. In contrast, isolated CH1 binds to F-actin with a similar efficiency as that of the full-length tandem CH domain. Thus, the obvious question that arises is why tandem CH domains require CH2, when their actin-binding efficiency is originating primarily from CH1. To answer, we probed the thermodynamic stabilities of individual CH domains. Isolated CH1 domain is unstable and is prone to serious aggregation. Isolated CH2 is very stable, even appears to be more stable than the full-length tandem CH domain. In addition, the CH2 domain, which is more stable, is less functional. These results indicate that the main function of CH2 is to stabilize CH1. Consistently, the proposed structure of utrophin’s tandem CH domain based on earlier X-ray studies indicates a close proximity between the C-terminal helix of CH2 and the N-terminal helix of CH1, and this helix in CH2 is more dynamic in the full-length protein when compared with that in the absence of CH1, suggesting the mechanism by which CH2 stabilizes CH1. These observations indicate that the two CH domains contribute differentially to the folding and function of tandem CH domains, although both domains essentially have the same native structure in the tandem CH domain. The N-terminal domain determines the function, whereas the C-terminal domain determines the stability. This work was funded by the AHA Grant 11SDG4880046.

scholarly journals Nuclear localization of a DNA-binding C-terminal domain from Balbiani ring coded secretory protein.

1988 ◽  
Vol 7 (12) ◽  
pp. 3881-3888 ◽  
Author(s):  
L. Botella ◽  
C. Grond ◽  
H. Saiga ◽  
J. E. Edström
Keyword(s):  
Dna Binding ◽  
Nuclear Localization ◽  
Secretory Protein ◽  
Balbiani Ring ◽  
Terminal Domain

scholarly journals A Possible Role for the Asymmetric C-Terminal Domain Dimer of Rous Sarcoma Virus Integrase in Viral DNA Binding

PLoS ONE ◽  
2013 ◽  
Vol 8 (2) ◽  
pp. e56892 ◽  
Author(s):  
Ke Shi ◽  
Krishan K. Pandey ◽  
Sibes Bera ◽  
Ajaykumar C. Vora ◽  
Duane P. Grandgenett ◽  
...  
Keyword(s):  
Dna Binding ◽  
Rous Sarcoma Virus ◽  
Viral Dna ◽  
Terminal Domain ◽  
Rous Sarcoma ◽  
Sarcoma Virus

scholarly journals 06-P045 A G11A mutation N-terminal to the polyalanine tract in HOXD13 causes limb malformations by altering both the stability and the DNA-binding functions of HOXD13

2009 ◽  
Vol 126 ◽  
pp. S133
Author(s):  
Nathalie Brison ◽  
Sebastian Fantini ◽  
Giulia Vaccari ◽  
Philippe Debeer ◽  
Vincenzo Zappavigna ◽  
...  
Keyword(s):  
Dna Binding ◽  
Limb Malformations ◽  
The Stability ◽  
Polyalanine Tract
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