scholarly journals Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system

2000 ◽  
Vol 267 (10) ◽  
pp. 2882-2889 ◽  
Author(s):  
Michel Neuburger ◽  
Ange M. Polidori ◽  
Emmanuel Piètre ◽  
Magali Faure ◽  
Agnés Jourdain ◽  
...  
Keyword(s):  
Glycine Decarboxylase ◽  
L Protein ◽  
Multienzyme System ◽  
Lipoamide Dehydrogenase ◽  
H Protein

Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system

2000 ◽  
Vol 267 (10) ◽  
pp. 2890-2898 ◽  
Author(s):  
Magali Faure ◽  
Jacques Bourguignon ◽  
Michel Neuburger ◽  
David Macherel ◽  
Larry Sieker ◽  
...  
Keyword(s):  
Glycine Decarboxylase ◽  
L Protein ◽  
Multienzyme System ◽  
Lipoamide Dehydrogenase ◽  
H Protein

Alternative splicing produces an H-protein with better substrate properties for the P-protein of glycine decarboxylase

FEBS Journal ◽  
2009 ◽  
Vol 276 (23) ◽  
pp. 6985-6991 ◽  
Author(s):  
Dirk Hasse ◽  
Stefan Mikkat ◽  
Martin Hagemann ◽  
Hermann Bauwe
Keyword(s):  
Alternative Splicing ◽  
Glycine Decarboxylase ◽  
P Protein ◽  
Substrate Properties ◽  
H Protein

scholarly journals Differential dynamics of neurofilament-H protein and neurofilament-L protein in neurons.

1994 ◽  
Vol 127 (1) ◽  
pp. 173-185 ◽  
Author(s):  
S Takeda ◽  
S Okabe ◽  
T Funakoshi ◽  
N Hirokawa
Keyword(s):  
Fluorescence Recovery After Photobleaching ◽  
The Other ◽  
Half Time ◽  
Dynamic Component ◽  
L Protein ◽  
The Core ◽  
Structural Specialization ◽  
H Protein

Neurofilaments (NFs) are composed of triplet proteins, NF-H, NF-M, and NF-L. To understand the dynamics of NFs in vivo, we studied the dynamics of NF-H and compared them to those of NF-L, using the combination of microinjection technique and fluorescence recovery after photobleaching. In the case of NF-L protein, the bleached zone gradually restored its fluorescence intensity with a recovery half time of approximately 35 min. On the other hand, recovery of the bleached zone of NF-H was considerably faster, taking place in approximately 19 min. However, in both cases the bleached zone was stationary. Thus, it was suggested that NF-H is the dynamic component of the NF array and is interchangeable, but that it assembles with the other neurofilament triplet proteins in a more exchangeable way, implying that the location of NF-H is in the periphery of the core NF array mainly composed of NF-L subunits. Immunoelectron microscopy investigations of the incorporation sites of NF-H labeled with biotin compounds also revealed the lateral insertion of NF-H subunits into the preexisting NF array, taking after the pattern seen in the case of NF-L. In summary, our results demonstrate that the dynamics of the L and H subunit proteins in situ are quite different from each other, suggesting different and separated mechanisms or structural specialization underlying the behavior of the two proteins.

scholarly journals Structural and Functional Characterization of H Protein Mutants of the Glycine Decarboxylase Complex

1999 ◽  
Vol 274 (37) ◽  
pp. 26344-26352 ◽  
Author(s):  
Virginie Gueguen ◽  
David Macherel ◽  
Michel Neuburger ◽  
Christine Saint Pierre ◽  
Michel Jaquinod ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Glycine Decarboxylase ◽  
Protein Mutants ◽  
Glycine Decarboxylase Complex ◽  
H Protein

scholarly journals Glycine decarboxylase and pyruvate dehydrogenase complexes share the same dihydrolipoamide dehydrogenase in pea leaf mitochondria: evidence from mass spectrometry and primary-structure analysis

1996 ◽  
Vol 313 (1) ◽  
pp. 229-234 ◽  
Author(s):  
Jacques BOURGUIGNON ◽  
Véronique MERAND ◽  
Stephen RAWSTHORNE ◽  
Eric FOREST ◽  
Roland DOUCE
Keyword(s):  
Pyruvate Dehydrogenase ◽  
Primary Structure ◽  
Polyclonal Antibodies ◽  
Pyruvate Dehydrogenase Complex ◽  
Spectrometric Analysis ◽  
Ionization Mass ◽  
Glycine Decarboxylase ◽  
Dihydrolipoamide Dehydrogenase ◽  
Terminal Sequence ◽  
L Protein

In order to compare the dihydrolipoamide dehydrogenase associated with the pyruvate dehydrogenase complex (E3) with that associated with the glycine decarboxylase complex (L-protein), we report for the first time the purification and characterization of the E3 component from pea leaf mitochondria. The first 30 amino acids of the N-terminal sequence of the mature E3 protein are identical with those of the mature L-protein of the glycine decarboxyase complex. Electrospray ionization-mass spectrometric analysis of E3 and the L-protein gave exactly the same molecular mass of 49753±5 Da. We have also confirmed the primary structure of the L-protein, in particular the C-terminal sequence, deduced from the cDNA published by Bourguignon, Macherel, Neuburger and Douce [(1992) Eur. J. Biochem. 204, 865-873]. Western-blot analysis shows that specific polyclonal antibodies raised against the L-protein recognize specifically both E3 and L-protein but not the porcine dihydrolipoamide dehydrogenase. We conclude that, in pea leaf mitochondria, the pyruvate dehydrogenase and glycine decarboxylase complexes share the same dihydrolipoamide dehydrogenase. We have also confirmed by MS analysis that the FAD is not covalently bound to the enzyme.

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