Roles of Charged Residues in the Conserved Motif, G-X-X-X-D/E-R/K-X-G-[X]-R/K-R/K, of the Lactose Permease of Escherichia coli

2000 ◽  
Vol 174 (1) ◽  
pp. 31-40 ◽  
Author(s):  
N.J. Pazdernik ◽  
E.A. Matzke ◽  
A.E. Jessen-Marshall ◽  
R.J. Brooker
Keyword(s):  
Escherichia Coli ◽  
Lactose Permease ◽  
Conserved Motif ◽  
Charged Residues

scholarly journals Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli.

1992 ◽  
Vol 89 (21) ◽  
pp. 10547-10551 ◽  
Author(s):  
M. Sahin-Toth ◽  
R. L. Dunten ◽  
A. Gonzalez ◽  
H. R. Kaback
Keyword(s):  
Escherichia Coli ◽  
Lactose Permease ◽  
Functional Interactions ◽  
Charged Residues

scholarly journals Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli.

1994 ◽  
Vol 269 (10) ◽  
pp. 7379-7386 ◽  
Author(s):  
P.J. Franco ◽  
R.J. Brooker
Keyword(s):  
Escherichia Coli ◽  
Lactose Permease ◽  
Functional Roles

Design of a membrane protein for site-specific proteolysis: properties of engineered factor Xa protease sites in the lactose permease of Escherichia coli

Biochemistry ◽  
1995 ◽  
Vol 34 (4) ◽  
pp. 1107-1112 ◽  
Author(s):  
Miklos Sahin-Toth ◽  
Rhonda L. Dunten ◽  
H. Ronald Kaback
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Factor Xa ◽  
Lactose Permease ◽  
Site Specific

scholarly journals Topography of lactose permease from Escherichia coli.

1988 ◽  
Vol 263 (31) ◽  
pp. 15906-15914 ◽  
Author(s):  
M G Page ◽  
J P Rosenbusch
Keyword(s):  
Escherichia Coli ◽  
Lactose Permease

scholarly journals Clusters of Charged Residues at the C Terminus of MotA and N Terminus of MotB Are Important for Function of the Escherichia coli Flagellar Motor

2008 ◽  
Vol 190 (15) ◽  
pp. 5517-5521 ◽  
Author(s):  
Edan R. Hosking ◽  
Michael D. Manson
Keyword(s):  
Escherichia Coli ◽  
Flagellar Motor ◽  
Protein Levels ◽  
Partner Protein ◽  
C Terminus ◽  
N Terminus ◽  
Charged Residues ◽  
Positively Charged ◽  
Terminal Cluster

ABSTRACT MotA contains a conserved C-terminal cluster of negatively charged residues, and MotB contains a conserved N-terminal cluster of positively charged residues. Charge-altering mutations affecting these residues impair motility but do not diminish Mot protein levels. The motility defects are reversed by second-site mutations targeting the same or partner protein.

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