Assembly and targeting of secretins in the bacterial outer membrane

被引：0
|
作者：
Natarajan, Janani [1 ]
Singh, Nidhi [2 ]
Rapaport, Doron [1 ]
机构：
[1] Univ Tubingen, Interfac Inst Biochem, Hoppe Seyler Str 4, D-72076 Tubingen, Germany
[2] Interfac Inst Microbiol & Infect Med IMIT, Elfriede Aulhorn Str 6, D-72076 Tubingen, Germany
来源：
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY | 2019年 / 309卷 / 07期
关键词：
Secretins; BAM complex; Gram-negative bacteria; Periplasmic chaperones; GRAM-NEGATIVE BACTERIA; II SECRETION; PSEUDOMONAS-AERUGINOSA; STRUCTURAL INSIGHTS; PILUS BIOGENESIS; NEISSERIA-MENINGITIDIS; PROTEIN SECRETION; TOXIN SECRETION; TERMINAL DOMAIN; INNER MEMBRANE;
D O I：
10.1016/j.ijmm.2019.06.002
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
In Gram-negative bacteria, secretion of toxins ensure the survival of the bacterium. Such toxins are secreted by sophisticated multiprotein systems. The most conserved part in some of these secretion systems are components, called secretins, which form the outer membrane ring in these systems. Recent structural studies shed some light on the oligomeric organization of secretins. However, the mechanisms by which these proteins are targeted to the outer membrane and assemble there into ring structures are still not fully understood. This review discusses the various species-specific targeting and assembly pathways that are taken by secretins in order to form their functional oligomers.
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页数：6
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