Adler L A, Arvidson S
Department of Bacteriology, Karolinska Institutet, Stockholm, Sweden.
J Gen Microbiol. 1987 Mar;133(3):803-13. doi: 10.1099/00221287-133-3-803.
The membrane-bound ribosome protein (MBRP)-complex of Staphylococcus aureus was studied using antibodies to its individual components. The four polypeptides of the complex were firmly held together, and none were present in large excess. The membrane-bound fraction of the MBRP-complex was accessible to trypsin only after removal of the membrane-bound ribosomes; it also remained associated with the membrane-bound ribosomes even after solubilization of the membranes with Triton X-100. Furthermore, the amount of MBRP-complex in the membrane was proportional to the rate of exoprotein synthesis. These results strongly suggest a role for the MBRP-complex in protein secretion.
利用针对金黄色葡萄球菌膜结合核糖体蛋白（MBRP）复合物各个组分的抗体，对该复合物进行了研究。该复合物的四种多肽紧密结合在一起，没有一种大量过剩。只有在去除膜结合核糖体后，胰蛋白酶才能作用于MBRP复合物的膜结合部分；即使在用 Triton X-100 溶解膜后，它仍与膜结合核糖体相关联。此外，膜中MBRP复合物的量与外蛋白合成速率成正比。这些结果有力地表明MBRP复合物在蛋白质分泌中起作用。
