Resumen
This chapter presents the many known anomalies of Legionella Pneumophila (HtpB) and a historical perspective of the research that led to the establishment of HtpB as a moonlighting chaperonin. It focuses on HtpB's moonlighting functions in all the cellular compartments where this chaperonin is found. HtpB is the only chaperonin in L. pneumophila, and a portion of it resides in extracytoplasmic bacterial locations either as a membrane-associated, periplasmic, or surface-exposed protein, playing unique protein-folding independent roles in each of these compartments. In an attempt to explain the phenotypes induced by recombinant HtpB in yeast and mammalian cells, the chapter conducts a number of yeast two-hybrid screenings to identify potential eukaryotic protein partners of HtpB. This screening identified yeast S-adenosyl methionine decarboxylase (SAMDC) as a specific partner of HtpB. HtpB and GroEL differ in a total of 137 amino acid positions scattered throughout the entire protein.
Idioma original | English |
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Título de la publicación alojada | Moonlighting Proteins |
Subtítulo de la publicación alojada | Novel Virulence Factors in Bacterial Infections |
Editorial | Wiley-Blackwell |
Páginas | 111-134 |
Número de páginas | 24 |
ISBN (versión digital) | 9781118951149 |
ISBN (versión impresa) | 9781118951118 |
DOI | |
Estado | Published - oct. 3 2016 |
Nota bibliográfica
Publisher Copyright:© 2017 John Wiley & Sons, Inc.
ASJC Scopus Subject Areas
- General Biochemistry,Genetics and Molecular Biology