Pendrak M L, Perry R D
Department of Microbiology and Immunology, Louisiana State University Medical Center, Shreveport 71130.
Mol Microbiol. 1993 May;8(5):857-64. doi: 10.1111/j.1365-2958.1993.tb01632.x.
One characteristic of pigmented (Pgm+) cells of Yersinia pestis is the adsorption of sufficient quantities of exogenous haemin during growth at 26 degrees C to form dark-brown colonies. Carriage of the cloned haemin-storage (hms) locus in pHMS1 restores this phenotype to spontaneous Pgm- chromosomal deletion mutants of Y. pestis. We have mapped the location of the structural genes for four proteins encoded on pHMS1 using minicell, in vitro transcription/translation, and complementation analysis. The hmsH and hmsF genes encode 90 kDa and 72 kDa protein precursors processed to surface-exposed, outer membrane proteins of 86 kDa and 70 kDa, respectively. Beta-galactosidase positive MudII1734 insertions in hmsR suggest that it encodes a protein that is also essential for haemin storage. Finally, the structural gene for a 41 kDa protein lies distal to the hmsH gene but, unlike hmsH, hmsF, and hmsR, its expression is not essential for the Hms+ phenotype in Y. pestis.
鼠疫耶尔森氏菌色素沉着（Pgm+）细胞的一个特征是，在26摄氏度生长期间吸附足够量的外源性血红素，从而形成深棕色菌落。pHMS1中克隆的血红素储存（hms）基因座的携带，将此表型恢复给鼠疫耶尔森氏菌的自发Pgm-染色体缺失突变体。我们使用微小细胞、体外转录/翻译和互补分析，绘制了pHMS1上编码的四种蛋白质的结构基因的位置。hmsH和hmsF基因分别编码90 kDa和72 kDa的蛋白质前体，加工后成为表面暴露的86 kDa和70 kDa的外膜蛋白。hmsR中β-半乳糖苷酶阳性的MudII1734插入表明，它编码一种对血红素储存也必不可少的蛋白质。最后，一种41 kDa蛋白质的结构基因位于hmsH基因的远端，但与hmsH、hmsF和hmsR不同，其表达对鼠疫耶尔森氏菌的Hms+表型并非必不可少。
