A comparison of the primary structures of the two B800‐850‐apoproteins from wild‐type Rhodopseudomonas sphaeroides strain 2.4.1 and a carotenoidless mutant strain R26.1
- 1 October 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 175 (2) , 231-237
- https://doi.org/10.1016/0014-5793(84)80742-5
Abstract
The α‐ and β‐apoproteins from the B800‐850‐complex of Rhodopseudomonas sphaeroides strain 2.4.1 have been sequenced. These results have been compared with those previously obtained with the analogous antenna apoproteins from the carotenoidless mutant R26.1 [9]. The α‐apoproteins differ at position 24, where a valine residue present in the wild‐type sequence is replaced by a phenylalanine residue in the mutant. The α‐apoproteins differ at the N‐terminus. In the wild‐type β‐apoprotein some chains have methionine at the N‐terminus and some have an N‐terminal threonine, while in the mutant the N‐terminus is threonine.Keywords
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