| pubmed-article:9484453 | pubmed:abstractText | The cyanobacterium Synechocystis 6803 was engineered to produce a D1 protein where one or more of the N-terminal threonines at positions 2, 3 and 4 were replaced by other amino acid residues. No phenotypic effects were found for the T2S or T2L mutations, whereas the T2V, T2L;T4V and T2V;T3V;T4V mutations resulted in reduced photoautotrophic growth rate and oxygen evolving activity. The mutant strain T2V;T3V;T4V exhibited an oxygen evolution activity that was only half of that for the wild-type strain. Despite of that, both accumulation and stability of the D1 protein in the thylakoid membrane appeared unaffected in the mutant. | lld:pubmed |
