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Figure 1.
Figure 1. Schematic representation of RNase II and the deletion
derivatives constructed. The three putative domains predicted
for E. coli RNase II are represented as rectangles: CSD (gray),
RNB domain (white) and S1 domain (diagonal stripes), and a
black box at the N terminus of each enzyme represents the
His-tag fused. The amino acids at the limits of each domain are
indicated. For amino acid numbering, the sequence used as
template was the untagged wild-type RNase II. The four highly
conserved sequence motifs of the RNB domain (motif I to IV) are
also depicted. Restriction sites used for the mutant
construction are indicated, and those introduced by mutagenesis
are labeled with an asterisk (*). The region removed on each
deletion mutant is represented as a broken line and the
numbering corresponds to the residues limiting the deleted
region. On the right, the plasmid encoding each deletion mutant
is indicated, as well as the molecular mass of the mutant
protein and their solubility after IPTG induction: more than 50%
soluble (S), less than 50% soluble (I). On the left is shown
the name used for each deletion protein. Figure 1. Schematic
representation of RNase II and the deletion derivatives
constructed. The three putative domains predicted for E. coli
RNase II are represented as rectangles: CSD (gray), RNB domain
(white) and S1 domain (diagonal stripes), and a black box at the
N terminus of each enzyme represents the His-tag fused. The
amino acids at the limits of each domain are indicated. For
amino acid numbering, the sequence used as template was the
untagged wild-type RNase II. The four highly conserved sequence
motifs of the RNB domain (motif I to IV) are also depicted.
Restriction sites used for the mutant construction are
indicated, and those introduced by mutagenesis are labeled with
an asterisk (*). The region removed on each deletion mutant is
represented as a broken line and the numbering corresponds to
the residues limiting the deleted region. On the right, the
plasmid encoding each deletion mutant is indicated, as well as
the molecular mass of the mutant protein and their solubility
after IPTG induction: more than 50% soluble (S), less than 50%
soluble (I). On the left is shown the name used for each
deletion protein.
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