.beta. Subunit of rat liver mitochondrial ATP synthase: cDNA cloning, amino acid sequence, expression in Escherichia coli and structural relationship to adenylate kinase

Biochemistry ◽  
1988 ◽  
Vol 27 (2) ◽  
pp. 553-560 ◽  
Author(s):  
David N. Garboczi ◽  
Arthur H. Fox ◽  
Sandra L. Gerring ◽  
Peter L. Pedersen
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Cloning ◽  
Atp Synthase ◽  
Rat Liver ◽  
Adenylate Kinase ◽  
Beta Subunit ◽  
Expression In Escherichia Coli ◽  
Mitochondrial Atp Synthase

Complete amino acid sequence of subunit e of rat liver mitochondrial hydrogen ion-ATP synthase

Biochemistry ◽  
1992 ◽  
Vol 31 (49) ◽  
pp. 12451-12454 ◽  
Author(s):  
Tomihiko Higuti ◽  
Kayo Kuroiwa ◽  
Yoshihiro Kawamura ◽  
Yutaka Yoshihara
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Atp Synthase ◽  
Rat Liver ◽  
Hydrogen Ion ◽  
Complete Amino Acid Sequence ◽  
Subunit E

scholarly journals Expression in Escherichia coli and characterization of a reconstituted recombinant 7Fe ferredoxin from Desulfovibrio africanus

1996 ◽  
Vol 314 (1) ◽  
pp. 63-71 ◽  
Author(s):  
Johanneke L. H. BUSCH ◽  
Jacques L. J. BRETON ◽  
Barry M. BARTLETT ◽  
Richard JAMES ◽  
E. Claude HATCHIKIAN ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Magnetic Circular Dichroism ◽  
Wild Type ◽  
E Coli ◽  
Excess Iron ◽  
Expression In Escherichia Coli ◽  
Type D

Desulfovibrio africanus ferredoxin III is a monomeric protein (molecular mass of 6585 Da) that contains one [3Fe-4S]1+/0 and one [4Fe-4S]2+/1+ cluster when isolated aerobically. The amino acid sequence consists of 61 amino acids, including seven cysteine residues that are all involved in co-ordination to the clusters. In order to isolate larger quantities of D. africanus ferredoxin III, we have overexpressed it in Escherichia coli by constructing a synthetic gene based on the amino acid sequence of the native protein. The recombinant ferredoxin was expressed in E. coli as an apoprotein. We have reconstituted the holoprotein by incubating the apoprotein with excess iron and sulphide in the presence of a reducing agent. The reconstituted recombinant ferredoxin appeared to have a lower stability than that of wild-type D. africanus ferredoxin III. We have shown by low-temperature magnetic circular dichroism and EPR spectroscopy that the recombinant ferredoxin contains a [3Fe-4S]1+/0 and a [4Fe-4S]2+/1+ cluster similar to those found in native D. africanus ferredoxin III. These results indicate that the two clusters have been correctly inserted into the recombinant ferredoxin.

scholarly journals The Primary Structure of Escherichia coli RNA Polymerase. Nucleotide Sequence of the rpoB Gene and Amino-Acid Sequence of the beta-Subunit

1981 ◽  
Vol 116 (3) ◽  
pp. 621-629 ◽  
Author(s):  
Yury A. OVCHINNIKOV ◽  
Galina S. MONASTYRSKAYA ◽  
Valentin V. GUBANOV ◽  
Sergey O. GURYEV ◽  
Oleg Yu. CHERTOV ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Rna Polymerase ◽  
Primary Structure ◽  
Rpob Gene ◽  
Beta Subunit
Sign in / Sign up

Export Citation Format

Share Document