scholarly journals Structure of the Complex of the Colicin E2 R-domain and Its BtuB Receptor

2007 ◽  
Vol 282 (32) ◽  
pp. 23163-23170 ◽  
Author(s):  
Onkar Sharma ◽  
Eiki Yamashita ◽  
Mariya V. Zhalnina ◽  
Stanislav D. Zakharov ◽  
Kirill A. Datsenko ◽  
...  
Keyword(s):  
Colicin E2 ◽  
R Domain

NEO-PI-R Domain and Facet Scale Predictors of Achievement Dispositions

2000 ◽  
Author(s):  
Kelli Canada ◽  
Scott R. Ross ◽  
M. Karega Rausch
Keyword(s):  
R Domain

scholarly journals Analysis of the Genetic Variability of Virulence-Related Loci in Epidemic Clones of Methicillin-Resistant Staphylococcus aureus

2005 ◽  
Vol 49 (1) ◽  
pp. 366-379 ◽  
Author(s):  
A. R. Gomes ◽  
S. Vinga ◽  
M. Zavolan ◽  
H. de Lencastre
Keyword(s):  
Staphylococcus Aureus ◽  
Genetic Variability ◽  
Amino Acid Level ◽  
Point Of View ◽  
Sequence Motifs ◽  
Related Factors ◽  
Specific Sequence ◽  
Methicillin Resistant ◽  
Sequence Types ◽  
R Domain

ABSTRACT Methicillin-resistant Staphylococcus aureus (MRSA) isolates have previously been classified into major epidemic clonal types by pulsed-field gel electrophoresis in combination with multilocus sequence typing (MLST) and staphylococcal cassette chromosome mec typing. We aimed to investigate whether genetic variability in potentially polymorphic domains of virulence-related factors could provide another level of differentiation in a diverse collection of epidemic MRSA clones. The target regions of strains representative of epidemic clones and genetically related methicillin-susceptible S. aureus isolates from the 1960s that were sequenced included the R domains of clfA and clfB; the D, W, and M regions of fnbA and fnbB; and three regions in the agr operon. Sequence variation ranged from very conserved regions, such as those for RNAIII and the agr interpromoter region, to the highly polymorphic R regions of the clf genes. The sequences of the clf R domains could be grouped into six major sequence types on the basis of the sequences in their 3′ regions. Six sequence types were also observed for the fnb sequences at the amino acid level. From an evolutionary point of view, it was interesting that a small DNA stretch at the 3′ clf R-domain sequence and the fnb sequences agreed with the results of MLST for this set of strains. In particular, clfB R-domain sequences, which had a high discriminatory capacity and with which the types distinguished were congruent with those obtained by other molecular typing methods, have potential for use for the typing of S. aureus. Clone- and strain-specific sequence motifs in the clf and fnb genes may represent useful additions to a typing methodology with a DNA array.

scholarly journals Structure and Function of the CFTR Chloride Channel

1999 ◽  
Vol 79 (1) ◽  
pp. S23-S45 ◽  
Author(s):  
DAVID N. SHEPPARD ◽  
MICHAEL J. WELSH
Keyword(s):  
Cystic Fibrosis ◽  
Chloride Channel ◽  
Atp Hydrolysis ◽  
Current Knowledge ◽  
Structure And Function ◽  
Binding Domains ◽  
Transporter Family ◽  
Membrane Spanning ◽  
And Function ◽  
R Domain

Sheppard, David N., and Michael J. Welsh. Structure and Function of the CFTR Chloride Channel. Physiol. Rev. 79 , Suppl.: S23–S45, 1999. — The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique member of the ABC transporter family that forms a novel Cl− channel. It is located predominantly in the apical membrane of epithelia where it mediates transepithelial salt and liquid movement. Dysfunction of CFTR causes the genetic disease cystic fibrosis. The CFTR is composed of five domains: two membrane-spanning domains (MSDs), two nucleotide-binding domains (NBDs), and a regulatory (R) domain. Here we review the structure and function of this unique channel, with a focus on how the various domains contribute to channel function. The MSDs form the channel pore, phosphorylation of the R domain determines channel activity, and ATP hydrolysis by the NBDs controls channel gating. Current knowledge of CFTR structure and function may help us understand better its mechanism of action, its role in electrolyte transport, its dysfunction in cystic fibrosis, and its relationship to other ABC transporters.

Molecular characterisation of the colicin E2 operon and identification of its products

1985 ◽  
Vol 198 (3) ◽  
pp. 465-472 ◽  
Author(s):  
Stewart T. Cole ◽  
Brigitte Saint-Joanis ◽  
Anthony P. Pugsley
Keyword(s):  
Molecular Characterisation ◽  
Colicin E2

scholarly journals Computational Studies Reveal Phosphorylation-dependent Changes in the Unstructured R Domain of CFTR

2008 ◽  
Vol 378 (5) ◽  
pp. 1052-1063 ◽  
Author(s):  
Tamás Hegedűs ◽  
Adrian W.R. Serohijos ◽  
Nikolay V. Dokholyan ◽  
Lihua He ◽  
John R. Riordan
Keyword(s):  
Computational Studies ◽  
R Domain

scholarly journals YieJ (CbrC) Mediates CreBC-Dependent Colicin E2 Tolerance in Escherichia coli

2010 ◽  
Vol 192 (13) ◽  
pp. 3329-3336 ◽  
Author(s):  
S. James L. Cariss ◽  
Chrystala Constantinidou ◽  
Mala D. Patel ◽  
Yuiko Takebayashi ◽  
Jon L. Hobman ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Microarray Analysis ◽  
Gene Knockout ◽  
Inner Membrane ◽  
Two Component ◽  
Inner Membrane Protein ◽  
Colicin E2 ◽  
K 12

ABSTRACT Colicin E2-tolerant (known as Cet2) Escherichia coli K-12 mutants overproduce an inner membrane protein, CreD, which is believed to cause the Cet2 phenotype. Here, we show that overproduction of CreD in a Cet2 strain results from hyperactivation of the CreBC two-component regulator, but CreD overproduction is not responsible for the Cet2 phenotype. Through microarray analysis and gene knockout and overexpression studies, we show that overexpression of another CreBC-regulated gene, yieJ (also known as cbrC), causes the Cet2 phenotype.

Sign in / Sign up

Export Citation Format

Share Document