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Nucleoid-associated PhaF phasin drives intracellular location and segregation of polyhydroxyalkanoate granules in Pseudomonas putida KT2442.

Abstract：

:The PhaF is a nucleoid-associated like protein of Pseudomonas putida KT2442 involved in the polyhydroxyalkanoate (PHA) metabolism. Its primary structure shows two modular domains; the N-terminal PHA granule-binding domain (phasin domain) and the C-terminal half containing AAKP-like tandem repeats characteristic of the histone H1 family. Although the PhaF binding to PHA granules and its role as transcriptional regulator have been previously demonstrated, the cell physiology meaning of these properties remains unknown. This work demonstrates that PhaF plays a crucial role in granule localization within the cell. TEM and flow cytometry studies of cells producing granules at early growth stage demonstrated that PhaF directs the PHA granules to the centre of the cells, forming a characteristic needle array. Our studies demonstrated the existence of two markedly different cell populations in the strain lacking PhaF protein, i.e. cells with and without PHA. Complementation studies definitively demonstrated a key role of PhaF in granule segregation during the cell division ensuring the equal distribution of granules between daughter cells. In vitro studies showed that PhaF binds DNA through its C-terminal domain in a non-specific manner. All these findings suggested a main role of PhaF in PHA apparatus through interactions with the segregating chromosome.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Galán B,Dinjaski N,Maestro B,de Eugenio LI,Escapa IF,Sanz JM,García JL,Prieto MA

doi

10.1111/j.1365-2958.2010.07450.x

subject

Has Abstract

pub_date

2011-01-01 00:00:00

pages

402-18

issue

2

eissn

0950-382X

issn

1365-2958

journal_volume

79

pub_type

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