scholarly journals Thermodynamic Analysis of Protein-Membrane Interactions: The case of Octameric Mitochondrial Creatine Kinase

2010 ◽  
Vol 98 (3) ◽  
pp. 382a-383a
Author(s):  
Malgorzata Tokarska-Schlattner ◽  
Uwe Schlattner
Keyword(s):  
Creatine Kinase ◽  
Thermodynamic Analysis ◽  
Membrane Interactions ◽  
Mitochondrial Creatine Kinase ◽  
Protein Membrane

scholarly journals Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase

1989 ◽  
Vol 264 (5) ◽  
pp. 2890-2897
Author(s):  
R C Haas ◽  
C Korenfeld ◽  
Z F Zhang ◽  
B Perryman ◽  
D Roman ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Mitochondrial Creatine Kinase ◽  
Isolation And Characterization

Mitochondrial Creatine Kinase

JAMA ◽  
1980 ◽  
Vol 243 (20) ◽  
pp. 2058 ◽  
Author(s):  
C. Jack Bark
Keyword(s):  
Creatine Kinase ◽  
Mitochondrial Creatine Kinase

scholarly journals Dextran strongly increases the Michaelis constants of oxidative phosphorylation and of mitochondrial creatine kinase in heart mitochondria

1998 ◽  
Vol 254 (1) ◽  
pp. 172-180 ◽  
Author(s):  
Frank Norbert Gellerich ◽  
Fanny Dorine Laterveer ◽  
Bernard Korzeniewski ◽  
Stephan Zierz ◽  
Klaas Nicolay
Keyword(s):  
Creatine Kinase ◽  
Oxidative Phosphorylation ◽  
Heart Mitochondria ◽  
Mitochondrial Creatine Kinase ◽  
Michaelis Constants

Specific protein-membrane interactions promote packaging of metallo-β-lactamases into outer membrane vesicles

2021 ◽  
Author(s):  
Carolina López ◽  
Alessio Prunotto ◽  
Guillermo Bahr ◽  
Robert A. Bonomo ◽  
Lisandro J. González ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Electrostatic Interactions ◽  
Active Form ◽  
Membrane Vesicles ◽  
Specific Protein ◽  
Outer Membrane Vesicles ◽  
Soluble Enzyme ◽  
Membrane Interactions ◽  
Resistance Determinants ◽  
Protein Membrane

Outer membrane vesicles (OMVs) act as carriers of bacterial products such as plasmids and resistance determinants, including metallo-β-lactamases. The lipidated, membrane-anchored metallo-β-lactamase NDM-1 can be detected in Gram-negative OMVs. The soluble domain of NDM-1 also forms electrostatic interactions with the membrane. Herein, we show that these interactions promote its packaging into OMVs produced by Escherichia coli . We report that favorable electrostatic protein-membrane interactions are also at work in the soluble enzyme IMP-1, while being absent in VIM-2. These interactions correlate with an enhanced incorporation of IMP-1 compared to VIM-2 into OMVs. Disruption of these interactions in NDM-1 and IMP-1 impairs their inclusion into vesicles, confirming their role in defining the protein cargo in OMVs. These results also indicate that packaging of metallo-β-lactamases into vesicles in their active form is a common phenomenon that involves cargo selection based on specific molecular interactions.

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