Premium
THE STRUCTURE OF PHYCOBILISOMES IN MUTANTS OF Synechococcus sp. STRAIN PCC 7942 DEVOID OF SPECIFIC LINKER POLYPEPTIDES
Author(s) -
Bhalerao R. P.,
Collier J. L.,
Gustafsson P.,
Grossman A. R.
Publication year - 1995
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1995.tb03975.x
Subject(s) - phycobilisome , strain (injury) , chemistry , mutant , linker , biophysics , microbiology and biotechnology , biochemistry , cyanobacteria , biology , genetics , gene , bacteria , anatomy , computer science , operating system
— The effect of elimination of the 30, 33 and 9 kDa phycobilisome rod‐linker polypeptides on rod length was examined by electron microscopy of phycobilisomes isolated from wild‐type Synechococcus sp. strain PCC 7942 and from genetically engineered mutants with lesions in the genes encoding the rod‐linker polypeptides. The maximum rod length in the absence of the 33 kDa linker polypeptide was two phycocyanin hexamers, whereas rods with up to five hexamers were found in the mutant strain lacking the 30 kDa linker polypeptide. Elimination of the 9 kDa linker polypeptide did not have a significant effect on rod length. Finally, mutants lacking either the 30 or 33 kDa rod‐associated linker polypeptides had an increased number of rods that terminated with a phycocyanin trimer. These observations are discussed with respect to the role of the linker polypeptides in the biosynthesis of the rod substructure.