TY - JOUR
T1 - Genetic analysis of a 9 kDa phycocyanin-associated linker polypeptide
AU - de Lorimier, Robert
AU - Bryant, Donald A.
AU - Stevens, S. Edward
N1 - Funding Information:
This work was supported by grant No. DMB-8510770 from the National Science Foundation to R. de L. and S.E.S.; and by grants No. GM-31625 from the National Institutes of Health and No. 83-CRCR-!-1336 from the U.S. Department of Agriculture to D.A.B. We thank Gerard Guglielmi of the Institut Pasteur for assistance with electron microscopic characterization of phyco-bilisomes.
PY - 1990/8/9
Y1 - 1990/8/9
N2 - The gene encoding LR9, a 9 kDa phycocyanin-associated linker polypeptide, was cloned from the cyanobacterium Synechococcus sp. PCC 7002 (Agmenellum quadruplicatum PR-6). This gene, termed cpcD, was located immediately 3′ to cpcC, a gene which encodes another phycocyanin-associated linker, LR33. Mutation of cpcD by insertion led to the loss of LR9 as the only detectable change in phycobilisome composition. Cells and isolated phycobilisomes from the cpcD- strain did not detectably differ from the wild-type in absorption or steady-state fluorescence emission. Purified phycobilisomes from the wild-type and cpcD- strains were compared by electron microscopy. The number of phycocyanin discs in the rod substructures of the mutant was more variable than in the wild-type. Hence, one function of LR9 may be to minimize the heterogeneity of rod length, possibly by binding to the core-distal face of phycocyanin-LR33 complexes to prevent the tandem joining of such units. A mutant in which cpcD and cpcC-cpcD intergenic sequences are deleted shows a partial loss of LR33. Inverted repeats in this intergenic region may be required for optimal stability of the cpcC transcript.
AB - The gene encoding LR9, a 9 kDa phycocyanin-associated linker polypeptide, was cloned from the cyanobacterium Synechococcus sp. PCC 7002 (Agmenellum quadruplicatum PR-6). This gene, termed cpcD, was located immediately 3′ to cpcC, a gene which encodes another phycocyanin-associated linker, LR33. Mutation of cpcD by insertion led to the loss of LR9 as the only detectable change in phycobilisome composition. Cells and isolated phycobilisomes from the cpcD- strain did not detectably differ from the wild-type in absorption or steady-state fluorescence emission. Purified phycobilisomes from the wild-type and cpcD- strains were compared by electron microscopy. The number of phycocyanin discs in the rod substructures of the mutant was more variable than in the wild-type. Hence, one function of LR9 may be to minimize the heterogeneity of rod length, possibly by binding to the core-distal face of phycocyanin-LR33 complexes to prevent the tandem joining of such units. A mutant in which cpcD and cpcC-cpcD intergenic sequences are deleted shows a partial loss of LR33. Inverted repeats in this intergenic region may be required for optimal stability of the cpcC transcript.
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U2 - 10.1016/0005-2728(90)90121-J
DO - 10.1016/0005-2728(90)90121-J
M3 - Article
C2 - 2118804
AN - SCOPUS:0025062807
VL - 1019
SP - 29
EP - 41
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
SN - 0005-2728
IS - 1
ER -