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J. Biol. Chem., Vol. 269, Issue 45, 27979-27986, 11, 1994
SY Kim, IG Kim, SI Chung and PM Steinert
Transglutaminase 1 (TGase1) is one of three known enzymes involved in
terminal differentiation in stratified squamous epithelia, possibly in the
formation of a cornified cell envelope. Because the intact enzyme is
particularly difficult to isolate in quantity from keratinocytes for
characterization, comparatively little is known about its properties. We
have expressed the full-length as well as a series of deletion forms of
this enzyme in a bacterial system and analyzed their enzymatic properties.
The specific activity of the full-length enzyme isolated and purified from
the bacterial lysate was comparable to that of the native enzyme of
keratinocytes. Analysis of several deletion constructs demonstrated that
removal of the first 60-109 residues, which include sequences involved in
membrane association, results in upwards of a 10- fold increase in the
specific activity. Deletions beyond residue 109, into sequences conserved
within the TGase family of proteins, result in loss of activity. Similarly,
as many as 240 residues can be removed from its carboxyl-terminal end
before activity is lost. Thus, a molecule of 466 residues, containing
virtually only the conserved core sequences of TGases, retains a specific
activity comparable to the intact enzyme. In addition, the various deletion
forms display wide variations in substrate specificity toward a series of
synthetic peptide substrates, designed from possible target TGase1
substrate proteins of epithelia. The data show that sequences between
residues 62 and 92 are important in defining the substrate specificity of
the TGase1 enzyme system. Furthermore, it may now be possible to design an
enzyme with a defined substrate specificity. Together, these data suggest
TGase1 has recruited additional sequences on its amino terminus in relation
to other members of the TGase family, which have the net effect of
permitting sequestration onto membranes, changing its specific activity and
modifying its likely substrate specificities.
The structure of the transglutaminase 1 enzyme. Deletion cloning reveals domains that regulate its specific activity and substrate specificity
Skin Biology Branch, NIAMS, National Institutes of Health, Bethesda, Maryland.
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