Plant Biology. In the article “Association of the Arabidopsis CTR1 Raf-like kinase with the ETR1 and ERS ethylene receptors” by Karen L. Clark, Paul B. Larsen, Xiaoxia Wang, and Caren Chang, which appeared in number 9, April 28, 1998, of Proc. Natl. Acad. Sci. USA (95, 5401–5406), the following correction should be noted. Fig. 5, accurately shown here, was damaged during the printing process.

Figure 5.

In vitro association of radiolabeled CTR1 polypeptides with purified MBP fusions: (i) MBP alone, (ii) MBP–ETR1^293–610, (iii) MBP–ETR1^604–738, and (iv) MBP-CKI1^981–1122. (A) Autoradiograms showing association of the CTR1 amino-terminal domain with MBP fusions 1–4. Bacterially expressed MBP or MBP fusion was attached to amylose-containing beads, and the beads were mixed with 5 or 25 μl of in vitro-translated, radiolabeled CTR1 amino-terminal domain (residues 53–568) (IVT). The bead-associated proteins were separated on SDS/PAGE gels, and the radiolabeled CTR1^53–568 was visualized by autoradiography. Lane IVT contains 0.1 μl of unassociated radiolabeled CTR1^53–568. (B) Autoradiogram showing association of the CTR1 kinase domain with MBP fusions 1–3. Bacterially expressed MBP or MBP fusion was attached to amylose-containing beads, and the beads were mixed with 5 μl of IVT. IVT in this case is the radiolabeled in vitro-translated CTR1 kinase domain (residues 538–821). The bead-associated proteins were subjected to SDS/PAGE, and radiolabeled CTR1^538–821 was visualized by autoradiography. Lane IVT contains 0.1 μl of unassociated radiolabeled CTR1^538–821. The length of exposure is twice that shown in Fig. 5A. (C) Relative amounts of MBP fusions 1–4 used in Fig. 5 A and B separated on SDS/PAGE gels and stained with Coomassie blue.