Zebrafish scarb2a insertional mutant reveals a novel function for the Scarb2/Limp2 receptor in notochord development

2016 ◽  
Vol 245 (4) ◽  
pp. 508-519 ◽  
Author(s):  
Abigail Diaz-Tellez ◽  
Cecilia Zampedri ◽  
Jose L. Ramos-Balderas ◽  
Fernando García-Hernández ◽  
Ernesto Maldonado
Keyword(s):  
Author(s):  
Cynthia J. Horst ◽  
Douglas J. Fishkind ◽  
Gregory J. Pazour ◽  
George B. Witman
Keyword(s):  

2000 ◽  
Vol 44 (6) ◽  
pp. 1745-1748 ◽  
Author(s):  
Genshi Zhao ◽  
Timothy I. Meier ◽  
Joann Hoskins ◽  
Kelly A. McAllister

ABSTRACT To further understand the role of penicillin-binding protein 2a (PBP 2a) of Streptococcus pneumoniae in penicillin resistance, we confirmed the identity of the protein as PBP 2a. The PBP 2a protein migrated electrophoretically to a position corresponding to that of PBP 2x, PBP 2a, and PBP 2b of S. pneumoniae and was absent in a pbp2ainsertional mutant of S. pneumoniae. We found that the affinities of PBP 2a for penicillins were lower than for cephalosporins and a carbapenem. When compared with other S. pneumoniae PBPs, PBP 2a exhibited lower affinities for β-lactam antibiotics, especially penicillins. Therefore, PBP 2a is a low-affinity PBP for β-lactam antibiotics in S. pneumoniae.


2016 ◽  
Vol 52 (3) ◽  
pp. 338-347 ◽  
Author(s):  
Anelia Iantcheva ◽  
Miglena Revalska ◽  
Grigor Zehirov ◽  
Irina Boycheva ◽  
Kevin Magne ◽  
...  

1990 ◽  
Vol 8 (4) ◽  
pp. 355-358 ◽  
Author(s):  
Anil K. Ratty ◽  
Lawrence W. Fitzgerald ◽  
Milt Titeler ◽  
Stanley D. Glick ◽  
John J. Mullins

1992 ◽  
Vol 3 (1) ◽  
pp. 5-10 ◽  
Author(s):  
Anik K. Ratty ◽  
Yoichi Matsuda ◽  
Rosemary W. Elliott ◽  
Verne M. Chapman ◽  
Kenneth W. Gross

Genomics ◽  
2007 ◽  
Vol 89 (4) ◽  
pp. 532-540 ◽  
Author(s):  
Chengkun He ◽  
Moul Dey ◽  
Zhihong Lin ◽  
Faping Duan ◽  
Fengling Li ◽  
...  

2010 ◽  
Vol 51 (3) ◽  
pp. 435-447 ◽  
Author(s):  
Benito Pineda ◽  
Estela Giménez-Caminero ◽  
Begoña García-Sogo ◽  
María Teresa Antón ◽  
Alejandro Atarés ◽  
...  

2002 ◽  
Vol 362 (3) ◽  
pp. 579-584 ◽  
Author(s):  
Monika SŁOMIṄSKA ◽  
Grażyna KONOPA ◽  
Grzegorz WĘGRZYN ◽  
Agata CZYŻ

The Vibrio harveyi cgtA gene product belongs to a subfamily of small GTP-binding proteins, called Obg-like proteins. Members of this subfamily are present in diverse organisms ranging from bacteria to humans. On the other hand, the functions of these proteins in the regulation of cellular processes are largely unknown. Genes coding for these proteins are essential in almost all bacteria investigated thus far. However, a viable V. harveyi insertional mutant in the cgtA gene was described recently. Therefore, this mutant gives a unique opportunity to study functions of a member of the subfamily of Obg-like proteins. Here we demonstrate that the mutant cells often form long filaments with expanded, non-partitioned or rarely partitioned chromosomes. Such a phenotype suggests impairment of the mechanism of chromosome partition. Flow cytometric studies revealed that synchronization of chromosome replication initiation is also significantly disturbed in the cgtA mutant. Moreover, in contrast to wild-type V. harveyi, inhibition of chromosome replication and/or of cell division in the mutant bacteria caused significant increase in the number of large cells, suggesting that the cgtA gene product may be involved in the coupling of cell growth to chromosome replication and cell division. These results indicate that CgtA, an Obg-like GTP-binding protein, plays an important role in the regulation of chromosomal functions.


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