Genome scale identification, structural analysis, and classification of periplasmic binding proteins from Mycobacterium tuberculosis

被引:3
作者
Sandhu, Padmani [1 ]
Kumari, Monika [1 ]
Naini, Kamal [1 ]
Akhter, Yusuf [1 ]
机构
[1] Cent Univ Himachal Pradesh, Sch Life Sci, Ctr Computat Biol & Bioinformat, Shahpur 176206, Himachal Prades, India
关键词
Periplasmic-binding proteins; Mycobacterium tuberculosis; Periplasm; Drug target; VII SECRETION SYSTEM; CRYSTAL-STRUCTURE; BIOCHEMICAL-CHARACTERIZATION; TRANSPORT MECHANISM; ESCHERICHIA-COLI; SIGNAL PEPTIDES; PREDICTION; CELL; SMEGMATIS; GENES;
D O I
10.1007/s00294-016-0664-5
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Periplasmic-binding proteins occupy the periplasmic space of bacteria and are involved in binding and transport of various ions, siderophores, and other diverse types of solutes. These proteins may be associated with membrane transport systems or may help in activation of signal transducers. There is limited information available on Mycobacterium tuberculosis (Mtb) periplasm-inhabiting proteins. In the present study, we have performed genome-wide identification and functional annotation of periplasmic-binding proteins of Mtb on the basis of signature characteristics and their functional motifs. 37 putative periplasmic-binding proteins were identified in Mtb proteome and categorized into different classes mainly known for their association with membrane transport and signaling pathways. Conclusively, this study adds 11 completely novel proteins to the periplasmic binding proteome of Mtb, which were not annotated as PBPs earlier. This study provides an overview of the periplasmic binding proteome of Mtb, which may be involved in various important patho-physiological functions of the bacteria. These proteins may serve as novel drug targets, which may lead to better treatment strategies against this deadly pathogen.
引用
收藏
页码:553 / 576
页数:24
相关论文
共 113 条
[41]   Bacterial growth and cell division: a mycobacterial perspective [J].
Hett, Erik C. ;
Rubin, Eric J. .
MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 2008, 72 (01) :126-+
[42]   ABC transporters: physiology, structure and mechanism - an overview [J].
Higgins, CF .
RESEARCH IN MICROBIOLOGY, 2001, 152 (3-4) :205-210
[43]   Holo-and apo-bound structures of bacterial periplasmic heme-binding proteins [J].
Ho, Winny W. ;
Li, Huiying ;
Eakanunkul, Suntara ;
Tong, Yong ;
Wilks, Angela ;
Guo, Maolin ;
Poulos, Thomas L. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (49) :35796-35802
[44]   Composition of the type VII secretion system membrane complex [J].
Houben, Edith N. G. ;
Bestebroer, Jovanka ;
Ummels, Roy ;
Wilson, Louis ;
Piersma, Sander R. ;
Jimenez, Connie R. ;
Ottenhoff, Tom H. M. ;
Luirink, Joen ;
Bitter, Wilbert .
MOLECULAR MICROBIOLOGY, 2012, 86 (02) :472-484
[45]   InterPro: the integrative protein signature database [J].
Hunter, Sarah ;
Apweiler, Rolf ;
Attwood, Teresa K. ;
Bairoch, Amos ;
Bateman, Alex ;
Binns, David ;
Bork, Peer ;
Das, Ujjwal ;
Daugherty, Louise ;
Duquenne, Lauranne ;
Finn, Robert D. ;
Gough, Julian ;
Haft, Daniel ;
Hulo, Nicolas ;
Kahn, Daniel ;
Kelly, Elizabeth ;
Laugraud, Aurelie ;
Letunic, Ivica ;
Lonsdale, David ;
Lopez, Rodrigo ;
Madera, Martin ;
Maslen, John ;
McAnulla, Craig ;
McDowall, Jennifer ;
Mistry, Jaina ;
Mitchell, Alex ;
Mulder, Nicola ;
Natale, Darren ;
Orengo, Christine ;
Quinn, Antony F. ;
Selengut, Jeremy D. ;
Sigrist, Christian J. A. ;
Thimma, Manjula ;
Thomas, Paul D. ;
Valentin, Franck ;
Wilson, Derek ;
Wu, Cathy H. ;
Yeats, Corin .
NUCLEIC ACIDS RESEARCH, 2009, 37 :D211-D215
[46]   Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold 'em, knowing when to fold 'em [J].
Hutchings, Matthew I. ;
Palmer, Tracy ;
Harrington, Dean J. ;
Sutcliffe, Iain C. .
TRENDS IN MICROBIOLOGY, 2009, 17 (01) :13-21
[47]   Mycobacterium tuberculosis RsdA provides a conformational rationale for selective regulation of σ-factor activity by proteolysis [J].
Jaiswal, Ravi K. ;
Prabha, Tangirala Surya ;
Manjeera, Gowravaram ;
Gopal, Balasubramanian .
NUCLEIC ACIDS RESEARCH, 2013, 41 (05) :3414-3423
[48]   Cj0011c, a periplasmic single- and double-stranded DNA-binding protein, contributes to natural transformation in Campylobacter jejuni [J].
Jeon, Byeonghwa ;
Zhang, Qijing .
JOURNAL OF BACTERIOLOGY, 2007, 189 (20) :7399-7407
[49]   Structural analysis of Mycobacterium tuberculosis ATP-binding cassette transporter subunit UgpB reveals specificity for glycerophosphocholine [J].
Jiang, Dunquan ;
Zhang, Qingqing ;
Zheng, Qianqian ;
Zhou, Hao ;
Jin, Jin ;
Zhou, Weihong ;
Bartlam, Mark ;
Rao, Zihe .
FEBS JOURNAL, 2014, 281 (01) :331-341
[50]   Prediction of lipoprotein signal peptides in Gram-negative bacteria [J].
Juncker, AS ;
Willenbrock, H ;
Von Heijne, G ;
Brunak, S ;
Nielsen, H ;
Krogh, A .
PROTEIN SCIENCE, 2003, 12 (08) :1652-1662