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Kicking MiD51 out of the enzyme club

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Two related proteins, MiD49 and MiD51, serve as Drp1’s receptors on the mitochondrial surface... Because Drp1 is a GTPase, the researchers wondered whether MiD51 was handing off GTP to its partner... However, neither GTP nor ATP bound to MiD51... On the other hand, the researchers found that MiD51 could bind GDP and ADP, yet these interactions weren’t necessary for mitochondrial fission... Nucleotidyltransferases carry a characteristic stretch of amino acids in their active site... All but one of these amino acids is missing from MiD51, indicating that the protein does not catalyze reactions... Instead, a region in MiD51 that is not usually found in other nucleotidyltransferases helps assemble the Drp1 molecular noose... When Richter et al. mutated this region, MiD51 was unable to connect to Drp1 and promote mitochondrial fission... The results suggest that MiD51 is a pseudoenzyme that reuses its nucleotidyltransferase fold as an assembly platform... Why MiD51 binds GDP and ADP is unclear, but one possibility is that they regulate the GTPase activity of Drp1.

No MeSH data available.


A time series shows a mitochondrion (red) splitting at the site of MiD51 binding (green).
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fig1: A time series shows a mitochondrion (red) splitting at the site of MiD51 binding (green).


Kicking MiD51 out of the enzyme club
A time series shows a mitochondrion (red) splitting at the site of MiD51 binding (green).
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3926953&req=5

fig1: A time series shows a mitochondrion (red) splitting at the site of MiD51 binding (green).

View Article: PubMed Central - HTML

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

Two related proteins, MiD49 and MiD51, serve as Drp1’s receptors on the mitochondrial surface... Because Drp1 is a GTPase, the researchers wondered whether MiD51 was handing off GTP to its partner... However, neither GTP nor ATP bound to MiD51... On the other hand, the researchers found that MiD51 could bind GDP and ADP, yet these interactions weren’t necessary for mitochondrial fission... Nucleotidyltransferases carry a characteristic stretch of amino acids in their active site... All but one of these amino acids is missing from MiD51, indicating that the protein does not catalyze reactions... Instead, a region in MiD51 that is not usually found in other nucleotidyltransferases helps assemble the Drp1 molecular noose... When Richter et al. mutated this region, MiD51 was unable to connect to Drp1 and promote mitochondrial fission... The results suggest that MiD51 is a pseudoenzyme that reuses its nucleotidyltransferase fold as an assembly platform... Why MiD51 binds GDP and ADP is unclear, but one possibility is that they regulate the GTPase activity of Drp1.

No MeSH data available.