Kinetic and Ligand Binding Evidence for Two Heme A-Based Terminal Oxidases in Plasma Membranes from Bacillus subtilis

1993 ◽  
Vol 301 (1) ◽  
pp. 129-137 ◽  
Author(s):  
B.C. Hill ◽  
L. Vo ◽  
J. Albanese
Keyword(s):  
Bacillus Subtilis ◽  
Ligand Binding ◽  
Plasma Membranes ◽  
Terminal Oxidases

scholarly journals High-yield purification of cytochrome aa3 and cytochrome caa3 oxidases from Bacillus subtilis plasma membranes

1995 ◽  
Vol 309 (1) ◽  
pp. 279-283 ◽  
Author(s):  
W Henning ◽  
L Vo ◽  
J Albanese ◽  
B C Hill
Keyword(s):  
Bacillus Subtilis ◽  
Plasma Membranes ◽  
Sequence Data ◽  
High Yield ◽  
Cytochrome Aa3 ◽  
Quinol Oxidase ◽  
Terminal Oxidases ◽  
Aerobic Culture ◽  
Conventional Procedure ◽  
Molecular Masses

When grown in aerated shaking culture, Bacillus subtilis expresses two different haem A-containing terminal oxidases: cytochrome aa3-quinol oxidase and cytochrome caa3 oxidase. This paper describes a high-yield conventional procedure for purifying the two haem A-containing oxidases from the same aerobic culture of Bacillus subtilis. Yields of close to 40% of the total haem A are achieved and about 6 mg of each of the purified oxidases is obtained from 4 litres of liquid culture. Both of the purified enzymes have two subunits, with apparent molecular masses of 71.6 kDa and 34.3 kDa for the cytochrome caa3 oxidase, and 67.6 kDa and 37.2 kDa for aa3-quinol oxidase. These features are in agreement with the sequence data for the corresponding structural genes in the aa3 and caa3 operons of B. subtilis. Some spectral and enzymic features of the two purified oxidases are reported that are consistent with the inclusion of both of these enzymes as members of the cytochrome oxidase superfamily.

Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) beta

1995 ◽  
Vol 108 (10) ◽  
pp. 3267-3278 ◽  
Author(s):  
J.P. Evans ◽  
R.M. Schultz ◽  
G.S. Kopf
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Guinea Pig ◽  
Ligand Binding ◽  
Zona Pellucida ◽  
Plasma Membranes ◽  
Signal Sequence ◽  
Rgd Peptides ◽  
Mouse Sperm ◽  
Disintegrin Domain

The guinea pig sperm protein, PH-30 (also known as fertilin), is postulated to participate in the interaction between the sperm and egg plasma membranes. The beta subunit of guinea pig PH-30 (gpPH-30 beta) contains a domain with homology to disintegrins, snake venom proteins that bind to integrins via an integrin-binding domain containing the tripeptide RGD. This raises the question of whether an egg integrin serves as a receptor for PH-30. Although mouse eggs express integrin subunits, their role in mouse fertilization is unresolved. Therefore, we examined fertilization for two different hallmarks of integrin function, namely, dependence of ligand binding on divalent cations and the ability to inhibit ligand binding with RGD peptides. We demonstrate that sperm binding to zona pellucida-free eggs is supported by Ca2+, Mg2+, or Mn2+. Ca2+ was necessary and sufficient for sperm-egg fusion, with 2.5 mM Ca2+ being the most effective concentration. In addition, fertilization could be partially inhibited with various RGD peptides, which caused a decrease in sperm-egg fusion by 30–58%. This partial inhibition of fusion with RGD peptides prompted the cloning of the mouse homologue of gpPH-30 beta (hereafter referred to as mPH-30 beta) to determine if it possessed the tripeptide RGD or a different amino acid sequence in its disintegrin domain. mPH-30 beta, which is expressed during meiotic and post-meiotic phases of spermatogenesis, shares significant similarities to gpPH-30 beta throughout the length of the molecule, from the signal sequence to the cytoplasmic tail. The full-length deduced amino acid sequence of mPH-30 beta. The disintegrin domain of mPH-30 beta has the tripeptide QDE (instead of RGD) in its cell recognition region. Peptides containing this QDE sequence decrease the binding and fusion of sperm with zona pellucida-free eggs by approximately 70%, suggesting that the disintegrin domain of mPH-30 beta participates in the interaction between sperm and egg membranes.

Characterization of the receptor for glucagon-like peptide-1(7–36)amide on plasma membranes from rat insulinoma-derived cells by covalent cross-linking

1989 ◽  
Vol 2 (2) ◽  
pp. 93-98 ◽  
Author(s):  
R. Göke ◽  
T. Cole ◽  
J. M. Conlon
Keyword(s):  
Ligand Binding ◽  
Protein Complex ◽  
Plasma Membranes ◽  
Specific Binding ◽  
Binding Protein ◽  
Single Class ◽  
Intact Cells ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1 ◽  
Rat Insulinoma

ABSTRACT 125I-Labelled glucagon-like peptide-1(7–36)amide was cross-linked to a specific binding protein in plasma membranes prepared from RINm5F rat insulinoma-derived cells using disuccinimidyl suberate. Consistent with the presence of a single class of binding site on the surface of intact cells, only a single radiolabelled band at Mr 63 000 was identified by SDS-PAGE after solubilization of the ligand—binding protein complex. The band was not observed when 10 nm glucagon-like peptide-1(7–36)amide was included in the binding assay, but 1 μm concentrations of glucagon-like peptide1(1–36)amide, glucagon-like peptide-2 and glucagon did not decrease the intensity of labelling. No change in the mobility of the band was observed under reducing conditions, suggesting that the binding protein in the receptor is not attached to other subunits via disulphide bonds. In control incubations using plasma membranes from pig intestinal epithelial cells, which do not contain specific binding sites for glucagon-like peptide-1(7–36)amide, no cross-linked ligand-binding protein complex was observed.

scholarly journals Electron transfer and ligand binding in terminal oxidases Impact of recent structural information

FEBS Letters ◽  
1994 ◽  
Vol 350 (2-3) ◽  
pp. 164-168 ◽  
Author(s):  
M. Brunori ◽  
G. Antonini ◽  
A. Giuffre ◽  
F. Malatesta ◽  
F. Nicoletti ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Ligand Binding ◽  
Structural Information ◽  
Terminal Oxidases

scholarly journals Partitioning, diffusion, and ligand binding of raft lipid analogs in model and cellular plasma membranes

2012 ◽  
Vol 1818 (7) ◽  
pp. 1777-1784 ◽  
Author(s):  
Erdinc Sezgin ◽  
Ilya Levental ◽  
Michal Grzybek ◽  
Günter Schwarzmann ◽  
Veronika Mueller ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Plasma Membranes

scholarly journals Partitioning, Diffusion, and Ligand Binding of Raft Lipid Analogs in Model and Cellular Plasma Membranes

2012 ◽  
Vol 102 (3) ◽  
pp. 296a-297a
Author(s):  
Erdinc Sezgin ◽  
Ilya Levantal ◽  
Guenter Schwarzmann ◽  
Veronika Mueller ◽  
Alf Honigmann ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Plasma Membranes

Bacillus subtilis expresses two kinds of haem-A-containing terminal oxidases

1991 ◽  
Vol 197 (3) ◽  
pp. 699-705 ◽  
Author(s):  
Marko LAURAEUS ◽  
Tuomas HALTIA ◽  
Matti SARASTE ◽  
Marten WIKSTROM
Keyword(s):  
Bacillus Subtilis ◽  
Terminal Oxidases

scholarly journals Terminal Oxidases of Bacillus subtilisStrain 168: One Quinol Oxidase, Cytochromeaa3 or Cytochrome bd, Is Required for Aerobic Growth

2000 ◽  
Vol 182 (23) ◽  
pp. 6557-6564 ◽  
Author(s):  
Lena Winstedt ◽  
Claes von Wachenfeldt
Keyword(s):  
Bacillus Subtilis ◽  
Sequence Analysis ◽  
Terminal Oxidase ◽  
Rich Medium ◽  
Aerobic Growth ◽  
Quinol Oxidase ◽  
Terminal Oxidases ◽  
Cytochrome Bd ◽  
Heme Copper Oxidases ◽  
Quinol Oxidases

ABSTRACT The gram-positive endospore-forming bacterium Bacillus subtilis has, under aerobic conditions, a branched respiratory system comprising one quinol oxidase branch and one cytochrome oxidase branch. The system terminates in one of four alternative terminal oxidases. Cytochrome caa 3 is a cytochromec oxidase, whereas cytochrome bd and cytochromeaa 3 are quinol oxidases. A fourth terminal oxidase, YthAB, is a putative quinol oxidase predicted from DNA sequence analysis. None of the terminal oxidases are, by themselves, essential for growth. However, one quinol oxidase (cytochromeaa 3 or cytochrome bd) is required for aerobic growth of B. subtilis strain 168. Data indicating that cytochrome aa 3 is the major oxidase used by exponentially growing cells in minimal and rich medium are presented. We show that one of the two heme-copper oxidases, cytochrome caa 3 or cytochromeaa 3, is required for efficient sporulation ofB. subtilis strain 168 and that deletion of YthAB in a strain lacking cytochrome aa 3 makes the strain sporulation deficient.

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