Koyama Kohei, Tsuchiya Tohru, Akimoto Seiji, Yokono Makio, Miyashita Hideaki, Mimuro Mamoru
Department of Interdisciplinary Environment, Graduate School of Human and Environmental Studies, Kyoto University, Japan.
FEBS Lett. 2006 Jun 12;580(14):3457-61. doi: 10.1016/j.febslet.2006.04.098. Epub 2006 May 15.
Two new linker proteins were identified by peptide mass fingerprinting in phycobilisomes isolated from the cyanobacterium Gloeobacter violaceus PCC 7421. The proteins were products of glr1262 and glr2806. Three tandem phycocyanin linker motifs similar to CpcC were present in each. The glr1262 product most probably functions as a rod linker connecting phycoerythrin and phycocyanin, while the glr2806 product may function as a rod-core linker. We have designated these two proteins CpeG and CpcJ, respectively. The morphology of phycobilisomes in G. violaceus has been reported to be a bundle-like shape with six rods, consistent with the proposed functions of these linkers.
通过肽质量指纹图谱，在从蓝细菌紫球藻PCC 7421分离出的藻胆体中鉴定出两种新的连接蛋白。这些蛋白是glr1262和glr2806的产物。每种蛋白中都存在三个与CpcC相似的串联藻蓝蛋白连接基序。glr1262的产物很可能作为连接藻红蛋白和藻蓝蛋白的棒状连接蛋白发挥作用，而glr2806的产物可能作为棒状核心连接蛋白发挥作用。我们分别将这两种蛋白命名为CpeG和CpcJ。据报道，紫球藻中藻胆体的形态为具有六个棒状结构的束状形状，这与这些连接蛋白的推测功能一致。
