NMR resonance assignments of the lantibiotic immunity protein NisI from Lactococcus lactis

被引：3
作者：
Hacker, Carolin [1 ,2 ]
Christ, Nina Alexandra [1 ,2 ]
Duchardt-Ferner, Elke [1 ,2 ]
Korn, Sophie [1 ]
Berninger, Lucija [1 ]
Koetter, Peter [1 ]
Entian, Karl-Dieter [1 ]
Woehnert, Jens [1 ,2 ]
机构：
[1] Goethe Univ Frankfurt, Inst Mol Biowissensch, D-60438 Frankfurt, Germany
[2] Goethe Univ Frankfurt, Ctr Biomol Magnet Resonance BMRZ, D-60438 Frankfurt, Germany
来源：
BIOMOLECULAR NMR ASSIGNMENTS | 2015年 / 9卷 / 02期
关键词：
NMR-assignments; Triple resonance experiments; NisI; Lantibiotic immunity; Lantibiotic; Lanthipeptide; Nisin; LIPID-FREE NISI; BACILLUS-SUBTILIS; GENES; SPECTROSCOPY; EXPRESSION; EPIDERMIN; BACKBONE; REVEALS; SPAI;
D O I：
10.1007/s12104-015-9595-1
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
The lantibiotic nisin is a small antimicrobial peptide which acts against a wide range of Gram-positive bacteria. Nisin-producing Lactococcus lactis strains express four genes for self-protection against their own antimicrobial compound. This immunity system consists of the lipoprotein NisI and the ABC transporter NisFEG. NisI is attached to the outside of the cytoplasmic membrane via a covalently linked diacylglycerol anchor. Both the lipoprotein and the ABC transporter are needed for full immunity but the exact immunity mechanism is still unclear. To gain insights into the highly specific immunity mechanism of nisin producing strains on a structural level we present here the backbone resonance assignment of NisI (25.8 kDa) as well as the virtually complete H-1,N-15,C-13 chemical shift assignments for the isolated 12.7 kDa N-terminal and 14.6 kDa C-terminal domains of NisI.
引用
收藏
页码：293 / 297
页数：5
相关论文
共 50 条
  • [21] The First Structure of a Lantibiotic Immunity Protein, SpaI from Bacillus subtilis, Reveals a Novel Fold
    Christ, Nina A.
    Bochmann, Sophie
    Gottstein, Daniel
    Duchardt-Ferner, Elke
    Hellmich, Ute A.
    Duesterhus, Stefanie
    Koetter, Peter
    Guentert, Peter
    Entian, Karl-Dieter
    Woehnert, Jens
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2012, 287 (42) : 35286 - 35298
  • [22] NMR resonance assignments for the GSPII-C domain of the PilF ATPase from Thermus thermophilus in complex with c-di-GMP
    Keller, Heiko
    Kruse, Kerstin
    Averhoff, Beate
    Duchardt-Ferner, Elke
    Woehnert, Jens
    BIOMOLECULAR NMR ASSIGNMENTS, 2019, 13 (02) : 361 - 366
  • [23] Incorporating Triple Resonance Experiment Data Into NVR For NMR Protein Structure-Based Assignments
    Ekren, Seyma Nur
    Apaydin, Mehmet Serkan
    2014 22ND SIGNAL PROCESSING AND COMMUNICATIONS APPLICATIONS CONFERENCE (SIU), 2014, : 1926 - 1929
  • [24] Identification of the genes involved in the secretion and self-immunity of lacticin Q, an unmodified leaderless bacteriocin from Lactococcus lactis QU 5
    Iwatani, Shun
    Yoneyama, Fuminori
    Miyashita, Shiho
    Zendo, Takeshi
    Nakayama, Jiro
    Sonomoto, Kenji
    MICROBIOLOGY-SGM, 2012, 158 : 2927 - 2935
  • [25] The protein regulator ArgR and the sRNA derived from the 3′-UTR region of its gene, ArgX, both regulate the arginine deiminase pathway in Lactococcus lactis
    van der Meulen, Sjoerd Bouwe
    Hesseling-Meinders, Anne
    de Jong, Anne
    Kok, Jan
    PLOS ONE, 2019, 14 (06):
  • [26] Crystal structure of the receptor-binding protein head domain from Lactococcus lactis phage bIL170
    Ricagno, Stefano
    Campanacci, Valerie
    Blangy, Stephanie
    Spinelli, Silvia
    Tremblay, Denise
    Moineau, Sylvain
    Tegoni, Mariella
    Cambillau, Christian
    JOURNAL OF VIROLOGY, 2006, 80 (18) : 9331 - 9335
  • [27] Characterization of functional domains of lantibiotic-binding immunity protein, NukH, from Staphylococcus warneri ISK-1
    Okuda, K
    Aso, Y
    Nagao, J
    Shioya, K
    Kanemasa, Y
    Nakayama, J
    Sonomoto, K
    FEMS MICROBIOLOGY LETTERS, 2005, 250 (01) : 19 - 25
  • [28] NMR resonance assignments for the GSPII-C domain of the PilF ATPase from Thermus thermophilus in complex with c-di-GMP
    Heiko Keller
    Kerstin Kruse
    Beate Averhoff
    Elke Duchardt-Ferner
    Jens Wöhnert
    Biomolecular NMR Assignments, 2019, 13 : 361 - 366
  • [29] Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR
    Lu, George J.
    Opella, Stanley J.
    JOURNAL OF BIOMOLECULAR NMR, 2014, 58 (01) : 69 - 81
  • [30] Lactococcus lactis Delivery of Surface Layer Protein A Protects Mice from Colitis by Re-Setting Host Immune Repertoire
    Arukha, Ananta Prasad
    Freguia, Christian Furlan
    Mishra, Meerambika
    Jha, Jyoti K.
    Kariyawasam, Subhashinie
    Fanger, Neil A.
    Zimmermann, Ellen M.
    Fanger, Gary R.
    Sahay, Bikash
    BIOMEDICINES, 2021, 9 (09)
12345