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 Bacterioljournal_title
Journal of bacteriologyauthors
Willby MJ,Balish MF,Ross SM,Lee KK,Jordan JL,Krause DCdoi
10.1128/JB.186.24.8221-8228.2004keywords:
subject
Has Abstractpub_date
2004-12-01 00:00:00pages
8221-8issue
24eissn
0021-9193issn
1098-5530pii
186/24/8221journal_volume
186pub_type
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更新日期:1984-08-01 00:00:00