Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function

2013 ◽  
Vol 322 (6) ◽  
pp. 359-378 ◽  
Author(s):  
Özlem Tastan Bishop ◽  
Adrienne Lesley Edkins ◽  
Gregory Lloyd Blatch
Keyword(s):  
Domain Conservation

Structure of the Sulfolobus solfataricus α-Glucosidase: Implications for Domain Conservation and Substrate Recognition in GH31

2006 ◽  
Vol 358 (4) ◽  
pp. 1106-1124 ◽  
Author(s):  
Heidi A. Ernst ◽  
Leila Lo Leggio ◽  
Martin Willemoës ◽  
Gordon Leonard ◽  
Paul Blum ◽  
...  
Keyword(s):  
Substrate Recognition ◽  
Sulfolobus Solfataricus ◽  
Domain Conservation

Adjoint Aerodynamic Design Optimization for Blades in Multistage Turbomachines—Part I: Methodology and Verification

2010 ◽  
Vol 132 (2) ◽  
Author(s):  
D. X. Wang ◽  
L. He
Keyword(s):  
Finite Difference ◽  
Finite Difference Method ◽  
Design Optimization ◽  
Difference Method ◽  
Method Development ◽  
Adjoint Method ◽  
Flow Characteristics ◽  
Compressor Stage ◽  
Flow Domain ◽  
Domain Conservation

The adjoint method for blade design optimization will be described in this two-part paper. The main objective is to develop the capability of carrying out aerodynamic blading shape design optimization in a multistage turbomachinery environment. To this end, an adjoint mixing-plane treatment has been proposed. In the first part, the numerical elements pertinent to the present approach will be described. Attention is paid to the exactly opposite propagation of the adjoint characteristics against the physical flow characteristics, providing a simple and consistent guidance in the adjoint method development and applications. The adjoint mixing-plane treatment is formulated to have the two fundamental features of its counterpart in the physical flow domain: conservation and nonreflectiveness across the interface. The adjoint solver is verified by comparing gradient results with a direct finite difference method and through a 2D inverse design. The adjoint mixing-plane treatment is verified by comparing gradient results against those by the finite difference method for a 2D compressor stage. The redesign of the 2D compressor stage further demonstrates the validity of the adjoint mixing-plane treatment and the benefit of using it in a multi-bladerow environment.

scholarly journals EMS1 and BRI1 control separate biological processes via extracellular domain diversity and intracellular domain conservation

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Bowen Zheng ◽  
Qunwei Bai ◽  
Lei Wu ◽  
Huan Liu ◽  
Yuping Liu ◽  
...  
Keyword(s):  
Intracellular Signaling ◽  
Physcomitrella Patens ◽  
Land Plant ◽  
Biological Processes ◽  
Expression Domain ◽  
Intracellular Domain ◽  
Intracellular Signaling Pathway ◽  
Domain Conservation ◽  
Signaling Components ◽  
Early Land

Abstract In flowering plants, EMS1 (Excess Microsporocytes 1) perceives TPD1 (Tapetum Determinant 1) to specify tapeta, the last somatic cell layer nurturing pollen development. However, the signaling components downstream of EMS1 are relatively unknown. Here, we use a molecular complementation approach to investigate the downstream components in EMS1 signaling. We show that the EMS1 intracellular domain is functionally interchangeable with that of the brassinosteroid receptor BRI1 (Brassinosteroid Insensitive 1). Furthermore, expressing EMS1 together with TPD1 in the BRI1 expression domain could partially rescue bri1 phenotypes, and led to the dephosphorylation of BES1, a hallmark of active BRI1 signaling. Conversely, expressing BRI1 in the EMS1 expression domain could partially rescue ems1 phenotypes. We further show that PpEMS1 and PpTPD1 from the early land plant Physcomitrella patens could completely rescue ems1 and tpd1 phenotypes, respectively. We propose that EMS1 and BRI1 have evolved distinct extracellular domains to control different biological processes but can act via a common intracellular signaling pathway.

scholarly journals Frustulins: Domain Conservation in a Protein Family Associated with Diatom Cell Walls

1996 ◽  
Vol 239 (2) ◽  
pp. 259-264 ◽  
Author(s):  
Nils Kroger ◽  
Christian Bergsdorf ◽  
Manfred Sumper
Keyword(s):  
Cell Walls ◽  
Protein Family ◽  
Diatom Cell ◽  
Domain Conservation

scholarly journals Some properties of Reinhardt and Hartogs domains

2002 ◽  
Vol 24 (24) ◽  
pp. 07
Author(s):  
Ludmila Bourchtein ◽  
Andrei Bourchtein
Keyword(s):  
Power Series ◽  
Complex Variables ◽  
Several Complex Variables ◽  
Geometric Representation ◽  
Reinhardt Domain ◽  
Hartogs Domains ◽  
Domain Conservation

The domains of certain types, such as Reinhardt and Hartogs, are used in different problems of theory of functions of several complex variables. For instance, any power series of several complex variables converges in the complete logarithmically convex Reinhardt domain. Transformations of Reinhardt and Hartogs allow us to diminish the dimension of space and to consider some type of domains using its images. This allows the visibility of the geometric representation and the simplification of the study of properties of such domains. In this article we consider some properties of Reinhardt and Hartogs domains and transformations. The properties of domain conservation under Reinhardt transformation and convexity conservation under Reinhardt and Hartogs transformation are proved.

scholarly journals Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors

2009 ◽  
Vol 18 (11) ◽  
pp. 2252-2264 ◽  
Author(s):  
Bulat I. Khayrutdinov ◽  
Won Jin Bae ◽  
Young Mi Yun ◽  
Jie Hye Lee ◽  
Takashi Tsuyama ◽  
...  
Keyword(s):  
Winged Helix ◽  
Terminal Domain ◽  
Domain Conservation

scholarly journals The crystal structure of a bacterial Class II ketol-acid reductoisomerase: Domain conservation and evolution

2005 ◽  
Vol 14 (12) ◽  
pp. 3089-3100 ◽  
Author(s):  
Rajiv Tyagi ◽  
Stephane Duquerroy ◽  
Jorge Navaza ◽  
Luke W. Guddat ◽  
Ronald G. Duggleby
Keyword(s):  
Crystal Structure ◽  
Class Ii ◽  
Domain Conservation

scholarly journals New SHH and Known SIX3 Variants in a Series of Latin American Patients with Holoprosencephaly

2021 ◽  
pp. 1-15
Author(s):  
Viviane Freitas de Castro ◽  
Daniel Mattos ◽  
Flavia Martinez de Carvalho ◽  
Denise Pontes Cavalcanti ◽  
Milagros M. Duenas-Roque ◽  
...  
Keyword(s):  
Latin American ◽  
Sanger Sequencing ◽  
Phenotypic Variability ◽  
Phenotypic Expression ◽  
Driver Gene ◽  
Incomplete Penetrance ◽  
Phenotype Correlation ◽  
Pathogenic Variants ◽  
Facial Defects ◽  
Domain Conservation

Holoprosencephaly (HPE) is the failure of the embryonic forebrain to develop into 2 hemispheres promoting midline cerebral and facial defects. The wide phenotypic variability and causal heterogeneity make genetic counseling difficult. Heterozygous variants with incomplete penetrance and variable expressivity in the <i>SHH</i>, <i>SIX3</i>, <i>ZIC2</i>, and <i>TGIF1</i> genes explain ∼25% of the known causes of nonchromosomal HPE. We studied these 4 genes and clinically described 27 Latin American families presenting with nonchromosomal HPE. Three new <i>SHH</i> variants and a third known <i>SIX3</i> likely pathogenic variant found by Sanger sequencing explained 15% of our cases. Genotype-phenotype correlation in these 4 families and published families with identical or similar driver gene, mutated domain, conservation of residue in other species, and the type of variant explain the pathogenicity but not the phenotypic variability. Nine patients, including 2 with <i>SHH</i> pathogenic variants, presented benign variants of the <i>SHH</i>, <i>SIX3</i>, <i>ZIC2</i>, and <i>TGIF1</i> genes with potential alteration of splicing, a causal proposition in need of further studies. Finding more families with the same <i>SIX3</i> variant may allow further identification of genetic or environmental modifiers explaining its variable phenotypic expression.

scholarly journals Synapomorphic variations in the THAP domains of the human THAP protein family and its homologs

2021 ◽  
Author(s):  
Hiral M. Sanghavi ◽  
Sharmistha Majumdar
Keyword(s):  
Secondary Structure ◽  
Dna Sequences ◽  
Structure Prediction ◽  
Secondary Structure Prediction ◽  
Protein Family ◽  
Cellular Functions ◽  
Multiple Sequence ◽  
Future Studies ◽  
Amino Terminal ◽  
Domain Conservation

AbstractThe THAP (Thanatos-associated protein) domain is a DNA-binding domain which binds DNA via a zinc coordinating C2CH motif. Although THAP domains share a conserved structural fold, they bind different DNA sequences in different THAP proteins which in turn perform distinct cellular functions. In this study, we investigate (using multiple sequence alignment, in silico motif and secondary structure prediction) THAP domain conservation within the homologs of the human THAP (hTHAP) protein family. We report that there is significant variation in sequence and predicted secondary structure elements across hTHAP homologs. Interestingly, we report that the THAP domain can be either longer or shorter than the conventional 90 residues and the amino terminal C2CH motif within the THAP domain serves as a hotspot for insertion or deletion. Our results lay the foundation for future studies which will further our understanding of the evolution of THAP domain and regulation of its function.

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