scholarly journals Escherichia coli Contains a Protein That Is Homologous in Function and N-terminal Sequence to the Protein Encoded by the nifS Gene of Azotobacter vinelandii and That Can Participate in the Synthesis of the Fe-S Cluster of Dihydroxy-acid Dehydratase

1996 ◽  
Vol 271 (27) ◽  
pp. 16068-16074
Author(s):  
Dennis H. Flint
Keyword(s):  
Escherichia Coli ◽  
Azotobacter Vinelandii ◽  
Terminal Sequence ◽  
Dihydroxy Acid ◽  
Acid Dehydratase

scholarly journals The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase

1993 ◽  
Vol 268 (20) ◽  
pp. 14732-14742
Author(s):  
D.H. Flint ◽  
M.H. Emptage ◽  
M.G. Finnegan ◽  
W. Fu ◽  
M.K. Johnson
Keyword(s):  
Escherichia Coli ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Dihydroxy Acid ◽  
Iron Sulfur ◽  
Acid Dehydratase

An activity stain for dihydroxy-acid dehydratase

1987 ◽  
Vol 164 (2) ◽  
pp. 526-530 ◽  
Author(s):  
Che Fu Kuo ◽  
Tadahiko Mashino ◽  
Irwin Fridovich
Keyword(s):  
Dihydroxy Acid ◽  
Acid Dehydratase

Interaction specificity between the chaperone and proteolytic components of the cyanobacterial Clp protease

2012 ◽  
Vol 446 (2) ◽  
pp. 311-320 ◽  
Author(s):  
Anders Tryggvesson ◽  
Frida M. Ståhlberg ◽  
Axel Mogk ◽  
Kornelius Zeth ◽  
Adrian K. Clarke
Keyword(s):  
Escherichia Coli ◽  
Active Sites ◽  
Terminal Sequence ◽  
Core Complex ◽  
Clp Protease ◽  
E Coli ◽  
Loop Region ◽  
N Terminus ◽  
Specific Association ◽  
The Stability

The Clp protease is conserved among eubacteria and most eukaryotes, and uses ATP to drive protein substrate unfolding and translocation into a chamber of sequestered proteolytic active sites. In plant chloroplasts and cyanobacteria, the essential constitutive Clp protease consists of the Hsp100/ClpC chaperone partnering a proteolytic core of catalytic ClpP and noncatalytic ClpR subunits. In the present study, we have examined putative determinants conferring the highly specific association between ClpC and the ClpP3/R core from the model cyanobacterium Synechococcus elongatus. Two conserved sequences in the N-terminus of ClpR (tyrosine and proline motifs) and one in the N-terminus of ClpP3 (MPIG motif) were identified as being crucial for the ClpC–ClpP3/R association. These N-terminal domains also influence the stability of the ClpP3/R core complex itself. A unique C-terminal sequence was also found in plant and cyanobacterial ClpC orthologues just downstream of the P-loop region previously shown in Escherichia coli to be important for Hsp100 association to ClpP. This R motif in Synechococcus ClpC confers specificity for the ClpP3/R core and prevents association with E. coli ClpP; its removal from ClpC reverses this core specificity.

Dihydroxy-acid dehydratase

1990 ◽  
pp. 617-621
Author(s):  
Dietmar Schomburg ◽  
Margit Salzmann
Keyword(s):  
Dihydroxy Acid ◽  
Acid Dehydratase

scholarly journals delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli.

1991 ◽  
Vol 173 (1) ◽  
pp. 94-100 ◽  
Author(s):  
G P O'Neill ◽  
S Thorbjarnardóttir ◽  
U Michelsen ◽  
S Pálsson ◽  
D Söll ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Aminolevulinic Acid ◽  
Acid Dehydratase
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