33kd actin binding protein which also hydrolyses DNA. So far DNase 1, together
with the ARP2/3 complex and tropomodulin is amongst the few ABPs to bind at the pointed end of actin
& Steck, 1988).
The physiological importance of the very tight association of DNAase
1 with actin is not certain as the two protein would not normally be expected to
meet, however such interaction has been reported in some cell types at least (Malickablaszkiewicz,
DNAase 1 has proved to be a valuable tool in the field as methods
have been developed which utilize the fact that when DNAase 1 is bound by actin
it no longer has the capacity to cleave DNA, in order to measure the G-actin
content of actin solutions (Fox
et al, 1981).
DNAase 1 played a vital part in the solution to the crystallographic structure of the actin monomer by preventing polymerization at high protein
et al, 1990),
the very high affinity of DNase 1 for actin was important in this regard.
DNase 1 has also been a very useful tool in the isolation of actin from various
sources by affiinity chomatography (Schafer
et al, 1998),
although it does not bind to actin from Entamoeba (Gadasi,
structure of DNase 1 (green)
in complex with actin (blue)
(Kabsch et al, 1990).
binds G-actin with very high affinity () at the "top" of sub-domain 2
(Figure 1) and to the pointed end of microfilaments with a Kd of
1.9x10-9 and an association rate constant of ~1x106 (Podolski
& Steck, 1988).
Not many other actin binding proteins bind to actin through this region (tropomodulin
and the ARP2/3 complex) and competition between DNase-1 and other ABPs does not
necessarily indicate competition for binding at this site since binding by
DNase-1 affects even the C terminus of the actin monomer (Usmanova
et al, 1997).
For example competition has been demonstrated between elongation factor 2 and
DNase-1 but it remains to be seen why this is the case (Bektas
et al, 1998).
DNase-1 also binds to some (Varma
et al, 1987) but not
all () actin related proteins.
of the DNase 1 family have been found to be be involved in DNA fragmentation
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