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Figure 5


Fig. 5. (A) Sequence alignment of the N-terminal domains of Glo3p, Gcs1p and rat Arfgap1. The ClustalW algorithm was used to create the alignment. Asterisks indicates positions that have a single, fully conserved residue; colons and stops indicate that the stronger- and weaker-score groups is fully conserved, respectively. SAT motifs (C2C2H2) (Zhang et al., 1998) are underlined, and the ArfGAP domain of rat Arfgap1 (residues 1-136) (Cukierman et al., 1995; Goldberg, 1999) is shaded. (B) Construction of chimeric proteins of Glo3p and Gcs1p. (C) Suppression activities of Glo3p and Gcs1p chimeric proteins. arf1-16 cells were transformed with pNY24-GLO3 (Glo3p), pNY24-GCS1-A-GLO3 (Gcs1-A-Glo3p), pNY24-GCS1-N-GLO3 (Gcs1-N-Glo3p), pNY24-GLO3-N-GCS1 (Glo3-N-Gcs1p), pNY24-GLO3-A-GCS1 (Glo3-A-Gcs1p), and pNY24-GCS1 (Gcs1p), and the transformants were grown at 23°C. Cells were diluted, spotted on MCD (-Trp) plates, and incubated at the indicated temperatures for 2 days. Integrants of wild-type ARF1 (WT) and mutants transformed with pYO324 (vector) were used as controls.





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