Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli

Biochemistry ◽  
1990 ◽  
Vol 29 (32) ◽  
pp. 7451-7459 ◽  
Author(s):  
Jochen Reinstein ◽  
Ilme Schlichting ◽  
Alfred Wittinghofer
2006 ◽  
Vol 188 (22) ◽  
pp. 7992-7996 ◽  
Author(s):  
Amrita Bharat ◽  
Mengxi Jiang ◽  
Susan M. Sullivan ◽  
Janine R. Maddock ◽  
Eric D. Brown

ABSTRACT To probe the cellular phenotype and biochemical function associated with the G domains of Escherichia coli EngA (YfgK, Der), mutations were created in the phosphate binding loop of each. Neither an S16A nor an S217A variant of G domain 1 or 2, respectively, was able to support growth of an engA conditional null. Polysome profiles of EngA-depleted cells were significantly altered, and His6-EngA was found to cofractionate with the 50S ribosomal subunit. The variants were unable to complement the abnormal polysome profile and were furthermore significantly impacted with respect to in vitro GTPase activity. Together, these observations suggest that the G domains have a cooperative function in ribosome stability and/or biogenesis.


Biochemistry ◽  
1992 ◽  
Vol 31 (2) ◽  
pp. 491-497 ◽  
Author(s):  
Christine R. Cremo ◽  
Joseph A. Loo ◽  
Charles G. Edmonds ◽  
Kristina M. Hatlelid

Biochemistry ◽  
1988 ◽  
Vol 27 (13) ◽  
pp. 4712-4720 ◽  
Author(s):  
Jochen Reinstein ◽  
Martin Brune ◽  
Alfred Wittinghofer

1987 ◽  
Vol 262 (6) ◽  
pp. 2502-2506
Author(s):  
M. Monnot ◽  
A.M. Gilles ◽  
I.S. Girons ◽  
S. Michelson ◽  
O. Bârzu ◽  
...  

1991 ◽  
Vol 266 (17) ◽  
pp. 10781-10786
Author(s):  
T. Rose ◽  
M. Brune ◽  
A. Wittinghofer ◽  
K. Le Blay ◽  
W.K. Surewicz ◽  
...  

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