scholarly journals Identification and Characterization of Multiple Osmotic Response Sequences in the Human Aldose Reductase Gene

1997 ◽  
Vol 272 (26) ◽  
pp. 16431-16437 ◽  
Author(s):  
Ben C. B. Ko ◽  
Barbara Ruepp ◽  
Kurt M. Bohren ◽  
Kenneth H. Gabbay ◽  
Stephen S. M. Chung
Diabetes ◽  
1992 ◽  
Vol 41 (9) ◽  
pp. 1165-1171 ◽  
Author(s):  
R. Kikkawa ◽  
K. Umemura ◽  
M. Haneda ◽  
N. Kajiwara ◽  
S. Maeda ◽  
...  

1993 ◽  
Vol 268 (21) ◽  
pp. 16052-16058
Author(s):  
K. Wang ◽  
K.M. Bohren ◽  
K.H. Gabbay

1994 ◽  
Vol 91 (22) ◽  
pp. 10742-10746 ◽  
Author(s):  
J. D. Ferraris ◽  
C. K. Williams ◽  
B. M. Martin ◽  
M. B. Burg ◽  
A. Garcia-Perez

1994 ◽  
Vol 92 (4) ◽  
pp. 613-623 ◽  
Author(s):  
Poul E. Jensen ◽  
Tine Hoff ◽  
Marianne G. Moller ◽  
Bjarne M. Stummann ◽  
Knud W. Henningsen

2005 ◽  
Vol 187 (3) ◽  
pp. 847-853 ◽  
Author(s):  
Ryo Endo ◽  
Mayuko Kamakura ◽  
Keisuke Miyauchi ◽  
Masao Fukuda ◽  
Yoshiyuki Ohtsubo ◽  
...  

ABSTRACT Sphingomonas paucimobilis UT26 utilizes γ-hexachlorocyclohexane (γ-HCH) as a sole source of carbon and energy. In our previous study, we cloned and characterized genes that are involved in the conversion of γ-HCH to maleylacetate (MA) via chlorohydroquinone (CHQ) in UT26. In this study, we identified and characterized an MA reductase gene, designated linF, that is essential for the utilization of γ-HCH in UT26. A gene named linEb, whose deduced product showed significant identity to LinE (53%), was located close to linF. LinE is a novel type of ring cleavage dioxygenase that catalyzes the conversion of CHQ to MA. LinEb expressed in Escherichia coli transformed CHQ and 2,6-dichlorohydroquinone to MA and 2-chloromaleylacetate, respectively. Our previous and present results indicate that UT26 (i) has two gene clusters for degradation of chlorinated aromatic compounds via hydroquinone-type intermediates and (ii) uses at least parts of both clusters for γ-HCH utilization.


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