Hanlon W A, Martinez-Canamero M, Inouye M, Inouye S
Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
J Bacteriol. 1995 Dec;177(24):7150-4. doi: 10.1128/jb.177.24.7150-7154.1995.
The mlpA gene encoding a 236-residue polypeptide has been identified immediately downstream of the oar gene of Myxococcus xanthus (M. Martinez-Canamero, J. Munoz-Dorado, E. Farez-Vidal, M. Inouye, and S. Inouye, J. Bacteriol. 175:4756-4763, 1993). The amino-terminal 21 residues of MlpA encode a typical prokaryotic signal sequence with a putative lipoprotein cleavage site. When expressed in Escherichia coli in the presence of [2-3H]glycerol, 3H-labeled MlpA had a molecular mass of 33 kDa and was found to be associated with the membrane fraction. Globomycin, an inhibitor of signal peptidase II, caused a shift in the mobility of E. coli-expressed MlpA to 35 kDa. Subsequently, a mlpA disruption strain (oar+) was constructed and found to have delayed fruiting body formation (by approximately 36 h), with significantly larger fruiting bodies being produced compared with those of the wild-type strain. Nevertheless, spore yields for the two strains were identical after 120 h of development. These data indicate that MlpA, the lipoprotein identified in M. xanthus, is required for normal fruiting body formation.
编码一种由236个氨基酸残基组成的多肽的mlpA基因,已在黄色粘球菌(M. Martinez-Canamero、J. Munoz-Dorado、E. Farez-Vidal、M. Inouye和S. Inouye,《细菌学杂志》175:4756 - 4763,1993年)的oar基因下游紧邻处被鉴定出来。MlpA的氨基末端21个残基编码一个具有假定脂蛋白切割位点的典型原核信号序列。当在含有[2 - 3H]甘油的情况下在大肠杆菌中表达时,3H标记的MlpA分子量为33 kDa,并且被发现与膜部分相关联。信号肽酶II的抑制剂globomycin导致大肠杆菌表达的MlpA迁移率发生变化,变为35 kDa。随后,构建了一个mlpA缺失菌株(oar +),发现其子实体形成延迟(约36小时),与野生型菌株相比,产生的子实体明显更大。然而,在发育120小时后,这两个菌株的孢子产量相同。这些数据表明,在黄色粘球菌中鉴定出的脂蛋白MlpA是正常子实体形成所必需的。