Dependence of secretion and assembly of type 1 fimbrial subunits of Escherichia coli on normal protein export

Dodd, D C; Bassford, P J; Eisenstein, B I

doi:10.1128/jb.159.3.1077-1079.1984

Cited by 37 publications

(7 citation statements)

References 13 publications

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“…Polymerisation of type I fimbriae from a relatively small intracellular pool takes about 3 min, and is considerably delayed when metabolic activity is reduced [380]. These fimbrial subunits may also have signal peptides, and seem to be channeled into the normal signal peptide pathway for protein export [381] (section 3).…”

Section: Surface Layers and Appendages And Other Examples Of Proteinmentioning

confidence: 99%

Export and secretion of proteins by bacteria

Pugsley

Schwartz

1985

FEMS Microbiology Letters

237

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A wide variety of proteins are exported or secreted by a range of morphologically distinct bacteria. The processes of protein export are most extensively characterised in Escherichia coli, where recent advances have been made in the identification of genes involved in forming the export machinery. Both Gram‐positive and Gram‐negative bacteria secrete proteins into the medium. Gram‐negative bacteria have adopted a variety of approaches in order to overcome the additional permeability of the outer membrane.

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Section: Surface Layers and Appendages And Other Examples Of Proteinmentioning

confidence: 99%

Export and secretion of proteins by bacteria

Pugsley

Schwartz

1985

FEMS Microbiology Letters

237

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“…Вопрос о том, как и каким образом этот процесс осуществляется, не обсуждался и не имеет научного объяснения. В то же время, присутствие ЛПС в составе капсулы могло быть случайным событием или же результатом активного транспорта ЛПС за пределы бактериальной клетки [13,25,28]. Анализ данных литературы об экспортирующих системах микроорганизмов и результаты собственных исследований позволили нам предположить, что процесс образования внеклеточной формы ЛПС функционально связан с активностью резидентных плазмид Y. pestis -pMT1, pCD1 и pPCP1.…”

Section: Rostov-on-don Research Institute For Plague Control Russiaunclassified

Yersinia pestis pathogenicity

Тынянова¹,

Sokolova²,

Зюзина³

et al. 2019

Journal of microbiology, epidemiology and immunobiology

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Ростовский-на Дону НИИ противочумный институт Yersinia pestis относится к числу патогенных бактерий, функцию токсина у которых выполняет структурный компонент клеточной стенки-липополисахарид (ЛПС). Для проявления токсического действия полимер должен быть отделен от внешней мембраны клетки и представлен рецепторам иммунокомпетентных клеток макроорганизма в функционально активной форме. В обзоре проанализирована и обобщена информация отечественных и зарубежных исследователей о токсигенных свойствах Y. pestis. Представлены результаты собственных экспериментов, которые свидетельствуют о том, что бактерии чумы способны экспортировать ЛПС в окружающую среду. Процесс является естественной функцией живой клетки, реализуется при температуре 37 0 С и строго зависит от экспрессии генов внехромосомных элементов наследственности Y. pestis-pMT1, pCD1, pPCP1. На примере изогенных вариантов вакцинного штамма Y. pestis EV76 и вирулентного штамма Y. pestis 231, содержащих различный набор плазмид, установлено, что максимальный вклад в активацию высокотемпературного ЛПС Y. pestis и переводу его в экстрацеллюлярную форму вносят белки плазмиды pCD1. Значение белка-«мышиного» токсина, кодируемого плазмидой pMT1, менее выражено. Участие плазмиды pPCP1 в проявление токсигенных свойств не обнаружено. Обсуждается роль капсульной субстанции Y. pestis и значение

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“…The products of all nine pap genes directly involved in P pilus biogenesis are synthesized as precursors containing classical N‐terminal SPs which direct them to the periplasmic space using the Sec‐machinery (GSP) to cross the cytoplasmic membrane [1]. Early work demonstrated the role of SecA protein and LepB signal peptidase in the secretion of type I fimbriae [84,85].…”

Section: Fimbriae (Pili)mentioning

confidence: 99%

Secretion and assembly of regular surface structures in Gram-negative bacteria

Fernández

Berenguer

2000

FEMS Microbiol Rev

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Bacteria synthesize large-sized surface structures through the ordered polymerization of protein subunits. This results in planar or tubular regular structures that have evolved to accomplish specific functions related to the particular environment in which these bacteria are found. Tubular assemblies known as flagella are the most complex structures known in bacteria and consist of a helical rigid filament, a torsion adapter or hook and a proton-fueled rotator known as the basal body. Pili or fimbriae are less complicated helical filaments, which consist of a major subunit and 3-5 minor subunits or pilins, whose main function is the attachment to specific surfaces. Planar structures known as S-layers are the simplest of these regular assemblies and are generally made up of a single subunit packed as a bidimensional crystal around the whole cell surface. Most of the components of these structures have to be secreted through the inner membrane (IM), the periplasm and the outer membrane (OM) before reaching their final destination. The so called general secretory pathway (GSP), or type II secretion system, appears to be implicated in this process to varying degrees, depending on the structure considered. A few S-layers and pili require GSP components but also need specific terminal branches, such as the well known chaperone-usher pathway. On the other hand, only two of the nearly 40 proteins involved in flagellar assembly are dependent on the GSP, while the external components are secreted through a specific pathway similar to the type III systems identified in some pathogens. Moreover, secretion of subunits of S-layers using dedicated type I machinery, without the involvement of any GSP component, has also been observed.

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Dependence of secretion and assembly of type 1 fimbrial subunits of Escherichia coli on normal protein export

Cited by 37 publications

References 13 publications

Export and secretion of proteins by bacteria

Export and secretion of proteins by bacteria

Yersinia pestis pathogenicity

Secretion and assembly of regular surface structures in Gram-negative bacteria

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