Metal-dependent SpoIIE oligomerization stabilizes FtsZ during asymmetric division in Bacillus subtilis

Ewa Król, Anabela de Sousa Borges, Malgorzata Kopacz, Dirk-Jan Scheffers

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

SpoIIE is a bifunctional protein involved in asymmetric septum formation and in activation of the forespore compartment-specific transcription factor σF through dephosphorylation of SpoIIAA-P. The phosphatase activity of SpoIIE requires Mn2+ as a metal cofactor. Here, we show that the presence of a metal cofactor also influences SpoIIE oligomerization and asymmetric septum formation. Absence of Mn2+ from sporulation medium results in a delay of the formation of polar FtsZ-rings, similar to a spoIIE null mutant. We purified the entire cytoplasmic part of the SpoIIE protein, and show that the protein copurifies with bound metals. Metal binding both stimulates SpoIIE oligomerization, and results in the formation of larger oligomeric structures. The presence of SpoIIE oligomers reduces FtsZ GTP hydrolysis activity and stabilizes FtsZ polymers in a light scattering assay. Combined, these results indicate that metal binding is not just required for SpoIIE phosphatase activity but also is important for SpoIIE's role in asymmetric septum formation.

OriginalsprogEngelsk
Artikelnummere0174713
TidsskriftPLOS ONE
Vol/bind12
Udgave nummer3
ISSN1932-6203
DOI
StatusUdgivet - 2017
Udgivet eksterntJa

Fingeraftryk

Oligomerization
Bacilli
Bacillus subtilis
Metals
metals
Phosphoric Monoester Hydrolases
Proteins
proteins
dephosphorylation
light scattering
Guanosine Triphosphate
sporulation
Oligomers
Light scattering
Hydrolysis
Assays
polymers
Polymers
Transcription Factors
transcription factors

Citer dette

Król, Ewa ; de Sousa Borges, Anabela ; Kopacz, Malgorzata ; Scheffers, Dirk-Jan. / Metal-dependent SpoIIE oligomerization stabilizes FtsZ during asymmetric division in Bacillus subtilis. I: PLOS ONE. 2017 ; Bind 12, Nr. 3.
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abstract = "SpoIIE is a bifunctional protein involved in asymmetric septum formation and in activation of the forespore compartment-specific transcription factor σF through dephosphorylation of SpoIIAA-P. The phosphatase activity of SpoIIE requires Mn2+ as a metal cofactor. Here, we show that the presence of a metal cofactor also influences SpoIIE oligomerization and asymmetric septum formation. Absence of Mn2+ from sporulation medium results in a delay of the formation of polar FtsZ-rings, similar to a spoIIE null mutant. We purified the entire cytoplasmic part of the SpoIIE protein, and show that the protein copurifies with bound metals. Metal binding both stimulates SpoIIE oligomerization, and results in the formation of larger oligomeric structures. The presence of SpoIIE oligomers reduces FtsZ GTP hydrolysis activity and stabilizes FtsZ polymers in a light scattering assay. Combined, these results indicate that metal binding is not just required for SpoIIE phosphatase activity but also is important for SpoIIE's role in asymmetric septum formation.",
keywords = "Bacillus subtilis, Bacterial Proteins, Cell Division, Cytoskeletal Proteins, Guanosine Triphosphate, Hydrolysis, Manganese, Metals, Protein Multimerization, Spores, Bacterial, Journal Article",
author = "Ewa Kr{\'o}l and {de Sousa Borges}, Anabela and Malgorzata Kopacz and Dirk-Jan Scheffers",
year = "2017",
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Metal-dependent SpoIIE oligomerization stabilizes FtsZ during asymmetric division in Bacillus subtilis. / Król, Ewa; de Sousa Borges, Anabela; Kopacz, Malgorzata; Scheffers, Dirk-Jan.

I: PLOS ONE, Bind 12, Nr. 3, e0174713, 2017.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Metal-dependent SpoIIE oligomerization stabilizes FtsZ during asymmetric division in Bacillus subtilis

AU - Król, Ewa

AU - de Sousa Borges, Anabela

AU - Kopacz, Malgorzata

AU - Scheffers, Dirk-Jan

PY - 2017

Y1 - 2017

N2 - SpoIIE is a bifunctional protein involved in asymmetric septum formation and in activation of the forespore compartment-specific transcription factor σF through dephosphorylation of SpoIIAA-P. The phosphatase activity of SpoIIE requires Mn2+ as a metal cofactor. Here, we show that the presence of a metal cofactor also influences SpoIIE oligomerization and asymmetric septum formation. Absence of Mn2+ from sporulation medium results in a delay of the formation of polar FtsZ-rings, similar to a spoIIE null mutant. We purified the entire cytoplasmic part of the SpoIIE protein, and show that the protein copurifies with bound metals. Metal binding both stimulates SpoIIE oligomerization, and results in the formation of larger oligomeric structures. The presence of SpoIIE oligomers reduces FtsZ GTP hydrolysis activity and stabilizes FtsZ polymers in a light scattering assay. Combined, these results indicate that metal binding is not just required for SpoIIE phosphatase activity but also is important for SpoIIE's role in asymmetric septum formation.

AB - SpoIIE is a bifunctional protein involved in asymmetric septum formation and in activation of the forespore compartment-specific transcription factor σF through dephosphorylation of SpoIIAA-P. The phosphatase activity of SpoIIE requires Mn2+ as a metal cofactor. Here, we show that the presence of a metal cofactor also influences SpoIIE oligomerization and asymmetric septum formation. Absence of Mn2+ from sporulation medium results in a delay of the formation of polar FtsZ-rings, similar to a spoIIE null mutant. We purified the entire cytoplasmic part of the SpoIIE protein, and show that the protein copurifies with bound metals. Metal binding both stimulates SpoIIE oligomerization, and results in the formation of larger oligomeric structures. The presence of SpoIIE oligomers reduces FtsZ GTP hydrolysis activity and stabilizes FtsZ polymers in a light scattering assay. Combined, these results indicate that metal binding is not just required for SpoIIE phosphatase activity but also is important for SpoIIE's role in asymmetric septum formation.

KW - Bacillus subtilis

KW - Bacterial Proteins

KW - Cell Division

KW - Cytoskeletal Proteins

KW - Guanosine Triphosphate

KW - Hydrolysis

KW - Manganese

KW - Metals

KW - Protein Multimerization

KW - Spores, Bacterial

KW - Journal Article

U2 - 10.1371/journal.pone.0174713

DO - 10.1371/journal.pone.0174713

M3 - Journal article

C2 - 28358838

VL - 12

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 3

M1 - e0174713

ER -