Cloning and genetic characterization of a calcium- and phospholipid-binding protein fromSaccharomyces cerevisiae that is homologous to translation elongation factor-1γ

Yeast ◽  
1993 ◽  
Vol 9 (2) ◽  
pp. 151-163 ◽  
Author(s):  
Nicholas G. Kambouris ◽  
Daniel J. Burke ◽  
Carl E. Creutz
FEBS Journal ◽  
2013 ◽  
Vol 280 (24) ◽  
pp. 6528-6540 ◽  
Author(s):  
Jennifer Doig ◽  
Lowri A. Griffiths ◽  
David Peberdy ◽  
Permphan Dharmasaroja ◽  
Maria Vera ◽  
...  

2012 ◽  
Vol 57 (9) ◽  
pp. 2347-2354 ◽  
Author(s):  
Xin Yu ◽  
Xiuxia Liu ◽  
Tiande Liu ◽  
Kui Hong ◽  
Jun Lei ◽  
...  

2017 ◽  
Vol 66 (4) ◽  
pp. 419-429 ◽  
Author(s):  
Sadegh Nouripour-Sisakht ◽  
Bahram Ahmadi ◽  
Koichi Makimura ◽  
Sybren de Hoog ◽  
Yoshiko Umeda ◽  
...  

2003 ◽  
Vol 19 (3) ◽  
pp. 231-237
Author(s):  
A. P. Pogrebnaya ◽  
N. V. Markeyeva ◽  
V. V. Lisogubov ◽  
A. M. Fridberg ◽  
S. I. Zabashnyi ◽  
...  

1993 ◽  
Vol 12 (1) ◽  
pp. 89-96 ◽  
Author(s):  
BARBARA PLAIMAUER ◽  
STEPHAN ORTNER ◽  
GERHARD WIEDERMANN ◽  
OTTO SCHEINER ◽  
MICHAEL DUCHÊNE

mBio ◽  
2017 ◽  
Vol 8 (5) ◽  
Author(s):  
Ralph Krafczyk ◽  
Jakub Macošek ◽  
Pravin Kumar Ankush Jagtap ◽  
Daniel Gast ◽  
Swetlana Wunder ◽  
...  

ABSTRACT Glycosylation is a universal strategy to posttranslationally modify proteins. The recently discovered arginine rhamnosylation activates the polyproline-specific bacterial translation elongation factor EF-P. EF-P is rhamnosylated on arginine 32 by the glycosyltransferase EarP. However, the enzymatic mechanism remains elusive. In the present study, we solved the crystal structure of EarP from Pseudomonas putida. The enzyme is composed of two opposing domains with Rossmann folds, thus constituting a B pattern-type glycosyltransferase (GT-B). While dTDP-β-l-rhamnose is located within a highly conserved pocket of the C-domain, EarP recognizes the KOW-like N-domain of EF-P. Based on our data, we propose a structural model for arginine glycosylation by EarP. As EarP is essential for pathogenicity in P. aeruginosa, our study provides the basis for targeted inhibitor design. IMPORTANCE The structural and biochemical characterization of the EF-P-specific rhamnosyltransferase EarP not only provides the first molecular insights into arginine glycosylation but also lays the basis for targeted-inhibitor design against Pseudomonas aeruginosa infection. IMPORTANCE The structural and biochemical characterization of the EF-P-specific rhamnosyltransferase EarP not only provides the first molecular insights into arginine glycosylation but also lays the basis for targeted-inhibitor design against Pseudomonas aeruginosa infection.


MycoKeys ◽  
2021 ◽  
Vol 80 ◽  
pp. 77-90
Author(s):  
Xianhong Wang ◽  
Yashuang Guo ◽  
Yamin Du ◽  
Ziling Yang ◽  
Xinzhong Huang ◽  
...  

Species of Diaporthe infect a wide range of plants and live in vivo as endophytes, saprobes or pathogens. However, those in peach plants are poorly characterized. In this study, 52 Diaporthe strains were isolated from peach branches with buds, showing constriction canker symptoms. Phylogenetic analyses were conducted using five gene regions: internal transcribed spacer of the ribosomal DNA (ITS), translation elongation factor 1-α (TEF), ß-tubulin (TUB), histone (HIS), and calmodulin (CAL). These results coupled with morphology revealed seven species of Diaporthe, including five known species (D. caryae, D. cercidis, D. eres, D. hongkongensis, and D. unshiuensis). In addition, two novel species D. jinxiu and D. zaofenghuang are introduced. Except for the previously reported D. eres, this study represents the first characterization of Diaporthe species associated with peach constriction canker in China, and contributes useful data for practicable disease management.


2007 ◽  
Vol 23 (5) ◽  
pp. 386-390 ◽  
Author(s):  
A. V. Novosylna ◽  
A. A. Timchenko ◽  
E. I. Tiktopulo ◽  
I. N. Serdyuk ◽  
B. S. Negrutskii ◽  
...  

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