A role for mechanosensitive channels in chloroplast and bacterial fission

Wilson, Margaret E.; Haswell, Elizabeth S.

doi:10.4161/psb.18735

Cited by 12 publications

(11 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This statement is also supported by the recently described observation that E . coli strain lacking both MscS and MscL channels, exhibited aberrant FtsZ ring assembly [ 73 ].…”

Section: Discussionmentioning

confidence: 99%

Cytoplasmic Domain of MscS Interacts with Cell Division Protein FtsZ: A Possible Non-Channel Function of the Mechanosensitive Channel in Escherichia Coli

et al. 2015

View full text Add to dashboard Cite

Bacterial mechano-sensitive (MS) channels reside in the inner membrane and are considered to act as emergency valves whose role is to lower cell turgor when bacteria enter hypo-osmotic environments. However, there is emerging evidence that members of the Mechano-sensitive channel Small (MscS) family play additional roles in bacterial and plant cell physiology. MscS has a large cytoplasmic C-terminal region that changes its shape upon activation and inactivation of the channel. Our pull-down and co-sedimentation assays show that this domain interacts with FtsZ, a bacterial tubulin-like protein. We identify point mutations in the MscS C-terminal domain that reduce binding to FtsZ and show that bacteria expressing these mutants are compromised in growth on sublethal concentrations of β-lactam antibiotics. Our results suggest that interaction between MscS and FtsZ could occur upon inactivation and/or opening of the channel and could be important for the bacterial cell response against sustained stress upon stationary phase and in the presence of β-lactam antibiotics.

show abstract

“…This statement is also supported by the recently described observation that E . coli strain lacking both MscS and MscL channels, exhibited aberrant FtsZ ring assembly [ 73 ].…”

Section: Discussionmentioning

confidence: 99%

Cytoplasmic Domain of MscS Interacts with Cell Division Protein FtsZ: A Possible Non-Channel Function of the Mechanosensitive Channel in Escherichia Coli

et al. 2015

View full text Add to dashboard Cite

show abstract

“…5), which is a feature of chloroplast division mutants (Osteryoung and Pyke, 2014). Curiously, mechanosensitive channels MSL2 and MSL3 at the chloroplast inner envelope were shown to be important for osmoregulation (Wilson et al, 2014), plastid division, and FtsZ division ring placement, although the mechanism is not clear (Wilson and Haswell, 2012). MSL2 and MSL3 show a similar patchy localization in mature chloroplasts (Haswell and Meyerowitz, 2006), as observed for AtKEA1 and AtKEA2 proteins.…”

Section: The Long N-terminal Domain Attaches Atkea1/2 To Specific Locmentioning

confidence: 93%

Envelope K⁺/H⁺ Antiporters AtKEA1 and AtKEA2 Function in Plastid Development

et al. 2016

View full text Add to dashboard Cite

It is well established that thylakoid membranes of chloroplasts convert light energy into chemical energy, yet the development of chloroplast and thylakoid membranes is poorly understood. Loss of function of the two envelope K + /H + antiporters AtKEA1 and AtKEA2 was shown previously to have negative effects on the efficiency of photosynthesis and plant growth; however, the molecular basis remained unclear. Here, we tested whether the previously described phenotypes of double mutant kea1kea2 plants are due in part to defects during early chloroplast development in Arabidopsis (Arabidopsis thaliana). We show that impaired growth and pigmentation is particularly evident in young expanding leaves of kea1kea2 mutants. In proliferating leaf zones, chloroplasts contain much lower amounts of photosynthetic complexes and chlorophyll. Strikingly, AtKEA1 and AtKEA2 proteins accumulate to high amounts in small and dividing plastids, where they are specifically localized to the two caps of the organelle separated by the fission plane. The unusually long amino-terminal domain of 550 residues that precedes the antiport domain appears to tether the full-length AtKEA2 protein to the two caps. Finally, we show that the double mutant contains 30% fewer chloroplasts per cell. Together, these results show that AtKEA1 and AtKEA2 transporters in specific microdomains of the inner envelope link local osmotic, ionic, and pH homeostasis to plastid division and thylakoid membrane formation.

show abstract

“…AtMSL10 channel has moderate selectivity for anions over cation with conductance of about 100 pS and reversibly inhibited by Gadolinium (Gd 3+ ) (Maksaev and Haswell, 2012). Similarly, AtMSL2 and AtMSL3 are localized in plastids and involved in various physiological activities such as maintenance of plastid shape and size, and placement of the divisional ring (Haswell and Meyerowitz, 2006;Wilson et al, 2011;Wilson and Haswell, 2012;Veley and Haswell, 2012). The functional analysis of Arabidopsis MSL2 showed that the conserved motif (PN (X) 9 N) are critical for maintenance of normal plastid and leaf morphology (Jensen and Haswell, 2012).…”

Section: Introductionmentioning

confidence: 99%

In silico identification and expression analysis of MscS like gene family in rice

Saddhe

Kumar

2015

Plant Gene

View full text Add to dashboard Cite

Mechanosensitive channels are membrane proteins that open and shut in response to mechanical forces produced by osmotic pressure, sound, touch and gravity. These channels are involved in multiple physiological functions including hypoosmotic pressure, pain, hearing, blood pressure and cell volume regulation. In plants, these channels play a major role in proprioception, gravity sensing and maintenance of plastid shape and size. In the present study, we identified the mechanosensitive channel of small conductance like (MscS) homologue gene family in rice and analyzed their structure, phylogenetic relationship, localization and expression pattern. Five MscS like genes of rice (OsMSL) were found to be distributed on four chromosomes and clustered into two major groups. Subcellular localization predictions of the OsMSL family revealed their localization to plasma membrane, plastid envelope and mitochondria. The predicted gene structure, bonafide conserved signature motif, domain and the presence of transmembrane regions in each OsMSL strongly supported their identity as members of MscS-like gene family. Furthermore, in silico expression analysis of OsMSL genes revealed differential regulation patterns in tissue specific and abiotic stress libraries. These findings indicate that the in silico approach used here successfully identified in a genome-wide context MscS like gene family in rice, and further suggest the functional importance of MscS-like genes in rice.

show abstract

A role for mechanosensitive channels in chloroplast and bacterial fission

Cited by 12 publications

References 26 publications

Cytoplasmic Domain of MscS Interacts with Cell Division Protein FtsZ: A Possible Non-Channel Function of the Mechanosensitive Channel in Escherichia Coli

Cytoplasmic Domain of MscS Interacts with Cell Division Protein FtsZ: A Possible Non-Channel Function of the Mechanosensitive Channel in Escherichia Coli

Envelope K⁺/H⁺ Antiporters AtKEA1 and AtKEA2 Function in Plastid Development

In silico identification and expression analysis of MscS like gene family in rice

Contact Info

Product

Resources

About

A role for mechanosensitive channels in chloroplast and bacterial fission

Cited by 12 publications

References 26 publications

Cytoplasmic Domain of MscS Interacts with Cell Division Protein FtsZ: A Possible Non-Channel Function of the Mechanosensitive Channel in Escherichia Coli

Cytoplasmic Domain of MscS Interacts with Cell Division Protein FtsZ: A Possible Non-Channel Function of the Mechanosensitive Channel in Escherichia Coli

Envelope K+/H+ Antiporters AtKEA1 and AtKEA2 Function in Plastid Development

In silico identification and expression analysis of MscS like gene family in rice

Contact Info

Product

Resources

About

Envelope K⁺/H⁺ Antiporters AtKEA1 and AtKEA2 Function in Plastid Development