HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae.

Abstract:

:The cytoskeletal proteins HMW1 and HMW2 are components of the terminal organelle of the cell wall-less bacterium Mycoplasma pneumoniae. HMW1 is required for a tapered, filamentous morphology but exhibits accelerated turnover in the absence of HMW2. Here, we report that a reciprocal dependency exists between HMW1 and HMW2, with HMW2 subject to accelerated turnover with the loss of HMW1. Furthermore, the instability of HMW2 correlated with its failure to localize to the attachment organelle. The C-terminal domain of HMW1 is essential for both function and its accelerated turnover in the absence of HMW2. We constructed HMW1 deletion derivatives lacking portions of this domain and examined each for stability and function. The C-terminal 41 residues were particularly important for proper localization and function in cell morphology and P1 localization, but the entire C-terminal domain was required to stabilize HMW2. The significance of these findings in the context of attachment organelle assembly is considered.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Willby MJ,Balish MF,Ross SM,Lee KK,Jordan JL,Krause DC

doi

10.1128/JB.186.24.8221-8228.2004

keywords:

subject

Has Abstract

pub_date

2004-12-01 00:00:00

pages

8221-8

issue

24

eissn

0021-9193

issn

1098-5530

pii

186/24/8221

journal_volume

186

pub_type

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