Site-directed mutagenesis of the CP 47 protein of photosystem II:167W in the lumenally exposed loop C is required for photosystem II assembly and stability

✍ Scribed by Jituo Wu; Cindy Putnam-Evans; Terry M. Bricker

• Publisher: Springer
• Year: 1996
• Tongue: English
• Weight: 632 KB
• Volume: 32
• Category: Article
• ISSN: 0167-4412
• DOI: 10.1007/bf00019106

✦ Synopsis

The intrinsic chlorophyll-protein CP 47 is a component of photosystem II which functions in both light-harvesting and oxygen evolution. Using site-directed mutagenesis we have produced the mutant W167S which lies in loop C of CP 47. This strain exhibited a 75% loss in oxygen evolution activity and grew extremely slowly in the absence of glucose. Examination of normalized oxygen evolution traces indicated that the mutant was susceptible to photoinactivation. Analysis of the variable fluorescence yield indicated that the mutant accumulated very few functional PS II reaction centers. This was confirmed by immunoblotting experiments. Interestingly, when W 167S was grown in the presence of 20 #M DCMU, the mutant continued to exhibit these defects. These results indicate that tryptophan 167 in loop C of CP 47 is important for the assembly and stability of the PS II reaction center.