MreB: Difference between revisions
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'''MreB''' is a protein found in bacteria that has been identified as a [[homology (biology)|homologue]] of [[actin]], as indicated by similarities in [[tertiary structure]] and conservation of active site [[amino acid sequence|peptide sequence]]. The conservation of protein structure suggests the [[common descent|common ancestry]] of the [[cytoskeleton|cytoskeletal]] elements formed by actin, found in [[eukaryote]]s, and MreB, found in [[prokaryote]]s.<ref name="pmid25788699">{{cite journal | vauthors = Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC | title = The evolution of compositionally and functionally distinct actin filaments | journal = Journal of Cell Science | volume = 128 | issue = 11 | pages = 2009–2019 | date = June 2015 | pmid = 25788699 | doi = 10.1242/jcs.165563 | doi-access = free }}</ref> Indeed, recent studies have found that MreB proteins [[polymerization|polymerize]] to form filaments that are similar to actin [[microfilament]]s. It has been shown to form multilayer sheets comprising diagonally interwoven filaments in the presence of ATP or GTP.<ref>{{cite journal | vauthors = Popp D, Narita A, Maeda K, Fujisawa T, Ghoshdastider U, Iwasa M, Maéda Y, Robinson RC | display-authors = 6 | title = Filament structure, organization, and dynamics in MreB sheets | journal = The Journal of Biological Chemistry | volume = 285 | issue = 21 | pages = 15858–15865 | date = May 2010 | pmid = 20223832 | pmc = 2871453 | doi = 10.1074/jbc.M109.095901 | doi-access = free }}</ref> | '''MreB''' is a protein found in bacteria that has been identified as a [[homology (biology)|homologue]] of [[actin]], as indicated by similarities in [[tertiary structure]] and conservation of active site [[amino acid sequence|peptide sequence]]. The conservation of protein structure suggests the [[common descent|common ancestry]] of the [[cytoskeleton|cytoskeletal]] elements formed by actin, found in [[eukaryote]]s, and MreB, found in [[prokaryote]]s.<ref name="pmid25788699">{{cite journal | vauthors = Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC | title = The evolution of compositionally and functionally distinct actin filaments | journal = Journal of Cell Science | volume = 128 | issue = 11 | pages = 2009–2019 | date = June 2015 | pmid = 25788699 | doi = 10.1242/jcs.165563 | doi-access = free }}</ref> Indeed, recent studies have found that MreB proteins [[polymerization|polymerize]] to form filaments that are similar to actin [[microfilament]]s. It has been shown to form multilayer sheets comprising diagonally interwoven filaments in the presence of ATP or GTP.<ref>{{cite journal | vauthors = Popp D, Narita A, Maeda K, Fujisawa T, Ghoshdastider U, Iwasa M, Maéda Y, Robinson RC | display-authors = 6 | title = Filament structure, organization, and dynamics in MreB sheets | journal = The Journal of Biological Chemistry | volume = 285 | issue = 21 | pages = 15858–15865 | date = May 2010 | pmid = 20223832 | pmc = 2871453 | doi = 10.1074/jbc.M109.095901 | doi-access = free }}</ref> | ||
MreB along with MreC and MreD are named after the mre operon ('''m'''u'''r'''ein formation gene cluster '''E''') to which they all belong.<ref>{{Cite book |last1=Löwe |first1=Jan |url=https://books.google.com/books?id=mDPbDgAAQBAJ&q=murein+formation+gene+cluster+E+MreB |title=Prokaryotic Cytoskeletons: Filamentous Protein Polymers Active in the Cytoplasm of Bacterial and Archaeal Cells |last2=Amos |first2=Linda A. |date=2017-05-11 |publisher=Springer |isbn=978-3-319-53047-5 | | MreB along with MreC and MreD are named after the mre operon ('''m'''u'''r'''ein formation gene cluster '''E''') to which they all belong.<ref>{{Cite book |last1=Löwe |first1=Jan |url=https://books.google.com/books?id=mDPbDgAAQBAJ&q=murein+formation+gene+cluster+E+MreB |title=Prokaryotic Cytoskeletons: Filamentous Protein Polymers Active in the Cytoplasm of Bacterial and Archaeal Cells |last2=Amos |first2=Linda A. |date=2017-05-11 |publisher=Springer |isbn=978-3-319-53047-5 |page=255 |language=en}}</ref> | ||
== Function == | == Function == | ||
MreB controls the width of rod-shaped [[bacteria]], such as ''[[Escherichia coli]]''. A [[mutant]] ''E. coli'' that creates defective MreB proteins will be spherical instead of rod-like. Also, most bacteria that are naturally spherical do not have the [[gene]] encoding MreB. Members of the [[Chlamydiota]] are a notable exception, as these bacteria utilize the protein for localized septal [[peptidoglycan]] synthesis.<ref>{{cite journal | vauthors = Ouellette SP, Karimova G, Subtil A, Ladant D | title = Chlamydia co-opts the rod shape-determining proteins MreB and Pbp2 for cell division | journal = Molecular Microbiology | volume = 85 | issue = 1 | pages = 164–178 | date = July 2012 | pmid = 22624979 | doi = 10.1111/j.1365-2958.2012.08100.x | s2cid = 5568586 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Liechti G, Kuru E, Packiam M, Hsu YP, Tekkam S, Hall E, Rittichier JT, VanNieuwenhze M, Brun YV, Maurelli AT | display-authors = 6 | title = Pathogenic Chlamydia Lack a Classical Sacculus but Synthesize a Narrow, Mid-cell Peptidoglycan Ring, Regulated by MreB, for Cell Division | journal = PLOS Pathogens | volume = 12 | issue = 5 | | MreB controls the width of rod-shaped [[bacteria]], such as ''[[Escherichia coli]]''. A [[mutant]] ''E. coli'' that creates defective MreB proteins will be spherical instead of rod-like. Also, most bacteria that are naturally spherical do not have the [[gene]] encoding MreB. Members of the [[Chlamydiota]] are a notable exception, as these bacteria utilize the protein for localized septal [[peptidoglycan]] synthesis.<ref>{{cite journal | vauthors = Ouellette SP, Karimova G, Subtil A, Ladant D | title = Chlamydia co-opts the rod shape-determining proteins MreB and Pbp2 for cell division | journal = Molecular Microbiology | volume = 85 | issue = 1 | pages = 164–178 | date = July 2012 | pmid = 22624979 | doi = 10.1111/j.1365-2958.2012.08100.x | s2cid = 5568586 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Liechti G, Kuru E, Packiam M, Hsu YP, Tekkam S, Hall E, Rittichier JT, VanNieuwenhze M, Brun YV, Maurelli AT | display-authors = 6 | title = Pathogenic Chlamydia Lack a Classical Sacculus but Synthesize a Narrow, Mid-cell Peptidoglycan Ring, Regulated by MreB, for Cell Division | journal = PLOS Pathogens | volume = 12 | issue = 5 | article-number = e1005590 | date = May 2016 | pmid = 27144308 | pmc = 4856321 | doi = 10.1371/journal.ppat.1005590 | doi-access = free }}</ref> [[Prokaryote]]s carrying the ''mreB'' gene can also be [[helix|helical]] in shape. MreB has long been thought to form a helical filament underneath the [[cytoplasmic membrane]], however, this model has been brought into question by three recent publications showing that filaments cannot be seen by electron cryotomography and that GFP-MreB can be seen as patches moving around the cell circumference. It has been shown to interact with several proteins that are proven to be involved in length growth (for instance [[Penicillin-binding proteins|PBP2]]). Therefore, it probably directs the synthesis and insertion of new [[peptidoglycan]] building units into the existing peptidoglycan layer to allow length growth of the bacteria. | ||
== References == | == References == | ||
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== Further reading == | == Further reading == | ||
{{refbegin}} | {{refbegin}} | ||
* {{cite journal | vauthors = Erickson HP | title = Cytoskeleton. Evolution in bacteria | journal = Nature | volume = 413 | issue = 6851 | | * {{cite journal | vauthors = Erickson HP | title = Cytoskeleton. Evolution in bacteria | journal = Nature | volume = 413 | issue = 6851 | page = 30 | date = September 2001 | pmid = 11544510 | doi = 10.1038/35092655 | s2cid = 4430479 | doi-access = free | bibcode = 2001Natur.413...30E }} - source of information added to this entry as of February 20, 2006 | ||
* {{cite journal | vauthors = Swulius MT, Chen S, Jane Ding H, Li Z, Briegel A, Pilhofer M, Tocheva EI, Lybarger SR, Johnson TL, Sandkvist M, Jensen GJ | display-authors = 6 | title = Long helical filaments are not seen encircling cells in electron cryotomograms of rod-shaped bacteria | journal = Biochemical and Biophysical Research Communications | volume = 407 | issue = 4 | pages = 650–655 | date = April 2011 | pmid = 21419100 | pmc = 3093302 | doi = 10.1016/j.bbrc.2011.03.062 }} | * {{cite journal | vauthors = Swulius MT, Chen S, Jane Ding H, Li Z, Briegel A, Pilhofer M, Tocheva EI, Lybarger SR, Johnson TL, Sandkvist M, Jensen GJ | display-authors = 6 | title = Long helical filaments are not seen encircling cells in electron cryotomograms of rod-shaped bacteria | journal = Biochemical and Biophysical Research Communications | volume = 407 | issue = 4 | pages = 650–655 | date = April 2011 | pmid = 21419100 | pmc = 3093302 | doi = 10.1016/j.bbrc.2011.03.062 }} | ||
* {{cite journal | vauthors = Domínguez-Escobar J, Chastanet A, Crevenna AH, Fromion V, Wedlich-Söldner R, Carballido-López R | title = Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria | journal = Science | volume = 333 | issue = 6039 | pages = 225–228 | date = July 2011 | pmid = 21636744 | doi = 10.1126/science.1203466 | s2cid = 45635270 | bibcode = 2011Sci...333..225D | url = https://hal.archives-ouvertes.fr/hal-01000382/file/PROGRESSIVA_1.pdf }} | * {{cite journal | vauthors = Domínguez-Escobar J, Chastanet A, Crevenna AH, Fromion V, Wedlich-Söldner R, Carballido-López R | title = Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria | journal = Science | volume = 333 | issue = 6039 | pages = 225–228 | date = July 2011 | pmid = 21636744 | doi = 10.1126/science.1203466 | s2cid = 45635270 | bibcode = 2011Sci...333..225D | url = https://hal.archives-ouvertes.fr/hal-01000382/file/PROGRESSIVA_1.pdf }} | ||
Latest revision as of 10:42, 30 September 2025
Template:More footnotes Template:Short description
Script error: No such module "Infobox".Template:Template other MreB is a protein found in bacteria that has been identified as a homologue of actin, as indicated by similarities in tertiary structure and conservation of active site peptide sequence. The conservation of protein structure suggests the common ancestry of the cytoskeletal elements formed by actin, found in eukaryotes, and MreB, found in prokaryotes.[1] Indeed, recent studies have found that MreB proteins polymerize to form filaments that are similar to actin microfilaments. It has been shown to form multilayer sheets comprising diagonally interwoven filaments in the presence of ATP or GTP.[2]
MreB along with MreC and MreD are named after the mre operon (murein formation gene cluster E) to which they all belong.[3]
Function
MreB controls the width of rod-shaped bacteria, such as Escherichia coli. A mutant E. coli that creates defective MreB proteins will be spherical instead of rod-like. Also, most bacteria that are naturally spherical do not have the gene encoding MreB. Members of the Chlamydiota are a notable exception, as these bacteria utilize the protein for localized septal peptidoglycan synthesis.[4][5] Prokaryotes carrying the mreB gene can also be helical in shape. MreB has long been thought to form a helical filament underneath the cytoplasmic membrane, however, this model has been brought into question by three recent publications showing that filaments cannot be seen by electron cryotomography and that GFP-MreB can be seen as patches moving around the cell circumference. It has been shown to interact with several proteins that are proven to be involved in length growth (for instance PBP2). Therefore, it probably directs the synthesis and insertion of new peptidoglycan building units into the existing peptidoglycan layer to allow length growth of the bacteria.
References
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Further reading
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- Script error: No such module "Citation/CS1". - source of information added to this entry as of February 20, 2006
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