红球菌MLDS蛋白的生物信息学分析  

Bioinformatics analysis of MLDS protein of Rhodococcus

作　　者：马学婧 王冠楠 曹春晖[1] 李雅君 杨晓童 马丽娜 周婷婷 杜晓娟 陈立凡 张子晗 宋立立[1] MA Xuejing;WANG Guannan;CAO Chunhui;LI Yajun;YANG Xiaotong;MA Lina;ZHOU Tingting;DU Xiaojuan;CHEN Lifan;ZHANG Zihan;SONG Lili(Department of Life Sciences,Cangzhou Normal University,Cangzhou,Hebei Province 061001,China;Office of Academic Research,Cangzhou Normal University,Cangzhou,Hebei Province 061001,China)

机构地区：[1]沧州师范学院生命科学系,河北沧州061001 [2]沧州师范学院科研处,河北沧州061001

出　　处：《中国饲料》2023年第15期52-57,98,共7页China Feed

基　　金：河北省教育厅科学技术研究项目(QN2020515);沧州师范学院校内科研基金项目(XNJJLQN2021002)。

摘　　要：为研究红球菌MLDS蛋白的结构特征,试验采用生物信息学方法对MLDS蛋白的理化性质、亲/疏水性、双亲性α螺旋、信号肽、跨膜区、二级结构、结构域、三级结构、重复序列、磷酸化位点进行了分析。结果显示:MLDS蛋白是稳定酸性亲水蛋白,N端存在一个双亲性α螺旋,没有信号肽和跨膜区,二级结构主要由α螺旋组成,具有Apolipoprotein结构域,三级结构由α螺旋束折叠而成,N端存在重复序列,共有20个潜在磷酸化位点。结果表明,MLDS蛋白是N端定位于脂滴的常驻蛋白,参与脂质代谢和DNA结合,是提高抗菌肽产量的潜在靶标。In order to explore the structural characteristics of MLDS protein of Rhodococcus,the physicochemical properties,hydrophilicity/hydrophobicity,amphipathicα-helix,signal peptide,transmembrane region,secondary structure,domain,tertiary structure,repeat sequence,and phosphorylation site of MLDS protein were investigated by bioinformatics methods.The results showed that the MLDS protein was a stable acidic hydrophilic protein with an amphipathicα-helix at the N-terminus,no signal peptide and transmembrane region,the secondary structure was mainly composed ofα-helix with an Apolipoprotein domain,and the tertiary structure was composed ofα-helix bundles.There were repeat sequences at the N-terminus and 20 potential phosphorylation sites.The results indicated that MLDS protein was a resident protein N-terminally localized to lipid droplets,participated in lipid metabolism and DNA binding,and was a potential target for improving the production of antimicrobial peptides.

关 键 词：MLDS蛋白 红球菌RHA1 抗菌肽 蛋白质结构 生物信息学分析 

分 类 号：S816.3[农业科学—饲料科学]