A cellulase/xylanase-negative mutant of Streptomyces lividans 1326 defective in cellobiose and xylobiose uptake is mutated in a gene encoding a protein homologous to ATP-binding proteins

1995 ◽  
Vol 17 (2) ◽  
pp. 367-377 ◽  
Author(s):  
Yves Hurtubise ◽  
François Shareck ◽  
Dieter Kluepfel ◽  
Rolf Morosoli
2000 ◽  
Vol 41 (3) ◽  
pp. 433-441
Author(s):  
Margaret E. Brousseau ◽  
Ernst J. Schaefer ◽  
Josee Dupuis ◽  
Brenda Eustace ◽  
Paul Van Eerdewegh ◽  
...  

2013 ◽  
Vol 85 (15) ◽  
pp. 7478-7486 ◽  
Author(s):  
Yongsheng Xiao ◽  
Lei Guo ◽  
Yinsheng Wang
Keyword(s):  

2007 ◽  
Vol 75 (6) ◽  
pp. 3188-3191 ◽  
Author(s):  
Kendra A. Hyland ◽  
Beinan Wang ◽  
P. Patrick Cleary

ABSTRACT Streptococcus pyogenes is a major cause of pharyngitis in humans and encodes several fibronectin-binding proteins. M protein and protein F1 (PrtF1/SfbI) are differentially regulated by CO2 and O2, respectively, and both mediate the invasion of epithelial cells. This study examined whether PrtF1/SfbI shares other properties with M protein. Expression of the PrtF1/SfbI protein by an M-negative mutant conferred resistance to phagocytosis and partial inhibition of C3 deposition on the S. pyogenes surface.


1999 ◽  
Vol 46 (2) ◽  
pp. 419-429 ◽  
Author(s):  
M Danieluk ◽  
R Buś ◽  
S Pikuła ◽  
J Bandorowicz-Pikuła

Annexin VI (AnxVI) from porcine liver, a member of the annexin family of Ca(2+)- and membrane-binding proteins, has been shown to bind ATP in vitro with a K(d) in the low micromolar concentration range. However, this protein does not contain within its primary structure any ATP-binding consensus motifs found in other nucleotide-binding proteins. In addition, binding of ATP to AnxVI resulted in modulation of AnxVI function, which was accompanied by changes in AnxVI affinity to Ca2+ in the presence of ATP. Using limited proteolytic digestion, purification of protein fragments by affinity chromatography on ATP-agarose, and direct sequencing, the ATP-binding site of AnxVI was located in a C-terminal half of the AnxVI molecule. To further study AnxVI-nucleotide interaction we have employed a functional nucleotide analog, Cibacron blue 3GA (CB3GA), a triazine dye which is commonly used to purify multiple ATP-binding proteins and has been described to modulate their activities. We have observed that AnxVI binds to CB3GA immobilized on agarose in a Ca(2+)-dependent manner. Binding is reversed by EGTA and by ATP and, to a lower extent, by other adenine nucleotides. CB3GA binds to AnxVI also in solution, evoking reversible aggregation of protein molecules, which resembles self-association of AnxVI molecules either in solution or on a membrane surface. Our observations support earlier findings that AnxVI is an ATP-binding protein.


2020 ◽  
Vol 31 (13) ◽  
pp. 1324-1345
Author(s):  
Sydney Skuodas ◽  
Amy Clemons ◽  
Michael Hayes ◽  
Ashley Goll ◽  
Betul Zora ◽  
...  

Skuodas and Clemons et al. show that protein aggregation is pervasive during early development and that the ABCF family of soluble ATP-binding proteins, which are encoded by animal genomes and expressed embryonically, regulate disaggregation and are instrumental for a normal developmental program.


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