Protein-protein interactions as determinants of operon architecture

Operons, clusters of genes under a single promoter, often exhibit a specific gene order influencing their physiological function. While functional relatedness is a known factor for clustering, the underlying drivers of gene ordering remain unclear. To investigate this, we analyzed the pdu operon, en...

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Published inBiochimica et biophysica acta. General subjects Vol. 1869; no. 6; p. 130794
Main Authors Bedi, Silky, Rose, S.M., Kaur, Simerpreet, Negi, Preeti, Sinha, Sharmistha
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.05.2025
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Abstract Operons, clusters of genes under a single promoter, often exhibit a specific gene order influencing their physiological function. While functional relatedness is a known factor for clustering, the underlying drivers of gene ordering remain unclear. To investigate this, we analyzed the pdu operon, encoding proteins for 1,2 Pdu bacterial microcompartment. Our bioinformatics revealed no link between the sequence similarity and proximity of the genes in the operon. However quantitative mapping of protein-protein interactions within the operon using a barrage of spectroscopic tools showed a strong correlation between interaction strength and gene proximity. Our data thus indicates that protein-protein interactions play a significant role in determining gene order within the pdu operon, potentially contributing to the efficient assembly and function of these microcompartments. [Display omitted] •Gene order in the pdu operon is optimized for assembly, with adjacent genes showing stronger protein interactions.•Strong protein interactions form nanotubes, while weaker ones lead to less defined assemblies.•The study offers a framework for bioengineering, enabling synthetic bacterial microcompartments.
AbstractList Operons, clusters of genes under a single promoter, often exhibit a specific gene order influencing their physiological function. While functional relatedness is a known factor for clustering, the underlying drivers of gene ordering remain unclear. To investigate this, we analyzed the pdu operon, encoding proteins for 1,2 Pdu bacterial microcompartment. Our bioinformatics revealed no link between the sequence similarity and proximity of the genes in the operon. However quantitative mapping of protein-protein interactions within the operon using a barrage of spectroscopic tools showed a strong correlation between interaction strength and gene proximity. Our data thus indicates that protein-protein interactions play a significant role in determining gene order within the pdu operon, potentially contributing to the efficient assembly and function of these microcompartments.
Operons, clusters of genes under a single promoter, often exhibit a specific gene order influencing their physiological function. While functional relatedness is a known factor for clustering, the underlying drivers of gene ordering remain unclear. To investigate this, we analyzed the pdu operon, encoding proteins for 1,2 Pdu bacterial microcompartment. Our bioinformatics revealed no link between the sequence similarity and proximity of the genes in the operon. However quantitative mapping of protein-protein interactions within the operon using a barrage of spectroscopic tools showed a strong correlation between interaction strength and gene proximity. Our data thus indicates that protein-protein interactions play a significant role in determining gene order within the pdu operon, potentially contributing to the efficient assembly and function of these microcompartments.Operons, clusters of genes under a single promoter, often exhibit a specific gene order influencing their physiological function. While functional relatedness is a known factor for clustering, the underlying drivers of gene ordering remain unclear. To investigate this, we analyzed the pdu operon, encoding proteins for 1,2 Pdu bacterial microcompartment. Our bioinformatics revealed no link between the sequence similarity and proximity of the genes in the operon. However quantitative mapping of protein-protein interactions within the operon using a barrage of spectroscopic tools showed a strong correlation between interaction strength and gene proximity. Our data thus indicates that protein-protein interactions play a significant role in determining gene order within the pdu operon, potentially contributing to the efficient assembly and function of these microcompartments.
Operons, clusters of genes under a single promoter, often exhibit a specific gene order influencing their physiological function. While functional relatedness is a known factor for clustering, the underlying drivers of gene ordering remain unclear. To investigate this, we analyzed the pdu operon, encoding proteins for 1,2 Pdu bacterial microcompartment. Our bioinformatics revealed no link between the sequence similarity and proximity of the genes in the operon. However quantitative mapping of protein-protein interactions within the operon using a barrage of spectroscopic tools showed a strong correlation between interaction strength and gene proximity. Our data thus indicates that protein-protein interactions play a significant role in determining gene order within the pdu operon, potentially contributing to the efficient assembly and function of these microcompartments. [Display omitted] •Gene order in the pdu operon is optimized for assembly, with adjacent genes showing stronger protein interactions.•Strong protein interactions form nanotubes, while weaker ones lead to less defined assemblies.•The study offers a framework for bioengineering, enabling synthetic bacterial microcompartments.
ArticleNumber 130794
Author Negi, Preeti
Rose, S.M.
Bedi, Silky
Sinha, Sharmistha
Kaur, Simerpreet
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Cites_doi 10.1128/JB.00785-16
10.1093/nar/gkae241
10.1016/j.saa.2012.02.088
10.1016/j.molcel.2010.04.008
10.1038/s41467-022-31279-3
10.1016/j.celrep.2015.12.085
10.1021/bi00745a020
10.1073/pnas.1207516109
10.1016/S0022-2836(61)80072-7
10.1039/C8RA00210J
10.1371/journal.pcbi.1004067
10.1126/science.aan3289
10.1371/journal.pcbi.1011038
10.1016/j.jmb.2020.11.020
10.1128/jb.00576-21
10.1039/D3TB00098B
10.1021/bi980274n
10.1128/JB.01473-10
10.3390/metabo5020252
10.1038/nrmicro787
10.1042/BST20170564
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Protein-protein interactions
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References Wells, Bergendahl, Marsh (bb0020) 2016; 14
Madeira, Madhusoodanan, Lee, Eusebi, Niewielska, Tivey, Lopez, Butcher (bb0025) 2024; 52
Perrin, Monod (bb0005) 1960; 29
Kennedy, Ikonomova, Slininger Lee, Raeder, Tullman-Ercek (bb0040) 2021; 433
Lakowicz, Weber (bb0065) 1973; 12
Parsons, Frank, Bhella, Liang, Prentice, Mulvihill, Warren (bb0075) 2010; 38
Sutter, Greber, Aussignargues, Kerfeld (bb0090) 2017; 356
Ewald, Kötzing, Bartl, Kaleta (bb0115) 2015; 5
Uddin, Frank, Warren, Pickersgill (bb0080) 2018; 14
Maity, Mukherjee, Das, Ghosh, Purkayastha (bb0055) 2012; 92
Jacob, Monod (bb0015) 1961; 3
Benni, Trabuco, Stasio, Arcovito, Boffi, Malatesta, Bonamore, Panfilis, de Turris, Baiocco (bb0030) 2018; 8
Rose, Radhakrishnan, Sinha (bb0070) 2023; 11
Garcia-Alles, Fuentes-Cabrera, Truan, Reguera (bb0095) 2023; 19
Mills, Waltmann, Archer, Kennedy, Abrahamson, Jackson, Roth, Shirman, Jewett, Mangan, Olvera de la Cruz, Tullman-Ercek (bb0050) 2022; 13
Cheng, Sinha, Fan, Liu, Bobik (bb0045) 2011; 193
Trettel, Winkler (bb0085) 2023; 11
Kennedy, Mills, Abrahamson, Archer, Shirman, Jewett, Mangan, Tullman-Ercek (bb0100) 2022; 204
Planamente, Frank (bb0105) 2019; 47
Browning, Busby (bb0010) 2004; 2
Chen, Barkley (bb0060) 1998; 37
Fan, Cheng, Sinha, Bobik (bb0110) 2012; 109
Jorda, Liu, Bobik, Yeates (bb0120) 2015; 11
Lehman, Chowdhury, Bobik (bb0035) 2017; 199
Jorda (10.1016/j.bbagen.2025.130794_bb0120) 2015; 11
Kennedy (10.1016/j.bbagen.2025.130794_bb0100) 2022; 204
Ewald (10.1016/j.bbagen.2025.130794_bb0115) 2015; 5
Parsons (10.1016/j.bbagen.2025.130794_bb0075) 2010; 38
Wells (10.1016/j.bbagen.2025.130794_bb0020) 2016; 14
Mills (10.1016/j.bbagen.2025.130794_bb0050) 2022; 13
Chen (10.1016/j.bbagen.2025.130794_bb0060) 1998; 37
Sutter (10.1016/j.bbagen.2025.130794_bb0090) 2017; 356
Jacob (10.1016/j.bbagen.2025.130794_bb0015) 1961; 3
Madeira (10.1016/j.bbagen.2025.130794_bb0025) 2024; 52
Kennedy (10.1016/j.bbagen.2025.130794_bb0040) 2021; 433
Garcia-Alles (10.1016/j.bbagen.2025.130794_bb0095) 2023; 19
Browning (10.1016/j.bbagen.2025.130794_bb0010) 2004; 2
Rose (10.1016/j.bbagen.2025.130794_bb0070) 2023; 11
Fan (10.1016/j.bbagen.2025.130794_bb0110) 2012; 109
Lehman (10.1016/j.bbagen.2025.130794_bb0035) 2017; 199
Lakowicz (10.1016/j.bbagen.2025.130794_bb0065) 1973; 12
Trettel (10.1016/j.bbagen.2025.130794_bb0085) 2023; 11
Uddin (10.1016/j.bbagen.2025.130794_bb0080) 2018; 14
Perrin (10.1016/j.bbagen.2025.130794_bb0005) 1960; 29
Maity (10.1016/j.bbagen.2025.130794_bb0055) 2012; 92
Benni (10.1016/j.bbagen.2025.130794_bb0030) 2018; 8
Cheng (10.1016/j.bbagen.2025.130794_bb0045) 2011; 193
Planamente (10.1016/j.bbagen.2025.130794_bb0105) 2019; 47
References_xml – volume: 13
  start-page: 3746
  year: 2022
  ident: bb0050
  article-title: Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology
  publication-title: Nat. Commun.
– volume: 12
  start-page: 4161
  year: 1973
  end-page: 4170
  ident: bb0065
  article-title: Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules
  publication-title: Biochemistry
– volume: 433
  year: 2021
  ident: bb0040
  article-title: Self-assembling Shell proteins PduA and PduJ have essential and redundant roles in bacterial microcompartment assembly
  publication-title: J. Mol. Biol.
– volume: 37
  start-page: 9976
  year: 1998
  end-page: 9982
  ident: bb0060
  article-title: Toward understanding tryptophan fluorescence in proteins
  publication-title: Biochemistry
– volume: 204
  year: 2022
  ident: bb0100
  article-title: Linking the Salmonella enterica 1,2-propanediol utilization bacterial microcompartment shell to the enzymatic core via the shell protein PduB
  publication-title: J. Bacteriol.
– volume: 356
  start-page: 1293
  year: 2017
  end-page: 1297
  ident: bb0090
  article-title: Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell
  publication-title: Science
– volume: 11
  start-page: 4842
  year: 2023
  end-page: 4854
  ident: bb0070
  article-title: Innate and engineered attributes of bacterial microcompartments for applications in bio-materials science
  publication-title: J. Mater. Chem. B
– volume: 2
  start-page: 57
  year: 2004
  end-page: 65
  ident: bb0010
  article-title: The regulation of bacterial transcription initiation
  publication-title: Nat. Rev. Microbiol.
– volume: 5
  start-page: 252
  year: 2015
  end-page: 269
  ident: bb0115
  article-title: Footprints of optimal protein assembly strategies in the operonic structure of prokaryotes
  publication-title: Metabolites
– volume: 11
  year: 2015
  ident: bb0120
  article-title: Exploring bacterial organelle Interactomes: a model of the protein-protein interaction network in the Pdu microcompartment
  publication-title: PLoS Comput. Biol.
– volume: 199
  year: 2017
  ident: bb0035
  article-title: The N terminus of the PduB protein binds the protein shell of the Pdu microcompartment to its enzymatic Core
  publication-title: J. Bacteriol.
– volume: 92
  start-page: 382
  year: 2012
  end-page: 387
  ident: bb0055
  article-title: Förster resonance energy transfer between pyrene and bovine serum albumin: effect of the hydrophobic pockets of cyclodextrins
  publication-title: Spectrochim. Acta A Mol. Biomol. Spectrosc.
– volume: 29
  start-page: 1727
  year: 1960
  end-page: 1729
  ident: bb0005
  article-title: The operon: a group of genes whose expression is coordinated by an operator
  publication-title: J. Bacteriol.
– volume: 109
  start-page: 14995
  year: 2012
  end-page: 15000
  ident: bb0110
  article-title: Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments
  publication-title: Proc. Natl. Acad. Sci.
– volume: 14
  start-page: 679
  year: 2016
  end-page: 685
  ident: bb0020
  article-title: Operon gene order is optimized for ordered protein complex assembly
  publication-title: Cell Rep.
– volume: 11
  start-page: e03357
  year: 2023
  end-page: e03422
  ident: bb0085
  article-title: In vitro analysis of bacterial microcompartments and Shell protein superstructures by confocal microscopy, microbiology
  publication-title: Spectrum
– volume: 19
  year: 2023
  ident: bb0095
  article-title: Inferring assembly-curving trends of bacterial micro-compartment shell hexamers from crystal structure arrangements
  publication-title: PLoS Comput. Biol.
– volume: 47
  start-page: 765
  year: 2019
  end-page: 777
  ident: bb0105
  article-title: Bio-engineering of bacterial microcompartments: a mini review
  publication-title: Biochem. Soc. Trans.
– volume: 14
  year: 2018
  ident: bb0080
  article-title: A generic self-assembly process in microcompartments and synthetic protein nanotubes
  publication-title: Small
– volume: 38
  start-page: 305
  year: 2010
  end-page: 315
  ident: bb0075
  article-title: Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement
  publication-title: Mol. Cell
– volume: 3
  start-page: 318
  year: 1961
  end-page: 356
  ident: bb0015
  article-title: Genetic regulatory mechanisms in the synthesis of proteins
  publication-title: J. Mol. Biol.
– volume: 8
  start-page: 12815
  year: 2018
  end-page: 12822
  ident: bb0030
  article-title: Excimer based fluorescent pyrene–ferritin conjugate for protein oligomerization studies and imaging in living cells
  publication-title: RSC Adv.
– volume: 193
  start-page: 1385
  year: 2011
  end-page: 1392
  ident: bb0045
  article-title: Genetic analysis of the protein shell of the microcompartments involved in coenzyme B12-dependent 1,2-propanediol degradation by Salmonella
  publication-title: J. Bacteriol.
– volume: 52
  start-page: W521
  year: 2024
  end-page: W525
  ident: bb0025
  article-title: The EMBL-EBI job dispatcher sequence analysis tools framework in 2024
  publication-title: Nucleic Acids Res.
– volume: 199
  year: 2017
  ident: 10.1016/j.bbagen.2025.130794_bb0035
  article-title: The N terminus of the PduB protein binds the protein shell of the Pdu microcompartment to its enzymatic Core
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.00785-16
– volume: 52
  start-page: W521
  year: 2024
  ident: 10.1016/j.bbagen.2025.130794_bb0025
  article-title: The EMBL-EBI job dispatcher sequence analysis tools framework in 2024
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkae241
– volume: 92
  start-page: 382
  year: 2012
  ident: 10.1016/j.bbagen.2025.130794_bb0055
  article-title: Förster resonance energy transfer between pyrene and bovine serum albumin: effect of the hydrophobic pockets of cyclodextrins
  publication-title: Spectrochim. Acta A Mol. Biomol. Spectrosc.
  doi: 10.1016/j.saa.2012.02.088
– volume: 38
  start-page: 305
  year: 2010
  ident: 10.1016/j.bbagen.2025.130794_bb0075
  article-title: Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2010.04.008
– volume: 13
  start-page: 3746
  year: 2022
  ident: 10.1016/j.bbagen.2025.130794_bb0050
  article-title: Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-022-31279-3
– volume: 14
  start-page: 679
  year: 2016
  ident: 10.1016/j.bbagen.2025.130794_bb0020
  article-title: Operon gene order is optimized for ordered protein complex assembly
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2015.12.085
– volume: 12
  start-page: 4161
  year: 1973
  ident: 10.1016/j.bbagen.2025.130794_bb0065
  article-title: Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules
  publication-title: Biochemistry
  doi: 10.1021/bi00745a020
– volume: 109
  start-page: 14995
  year: 2012
  ident: 10.1016/j.bbagen.2025.130794_bb0110
  article-title: Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments
  publication-title: Proc. Natl. Acad. Sci.
  doi: 10.1073/pnas.1207516109
– volume: 3
  start-page: 318
  year: 1961
  ident: 10.1016/j.bbagen.2025.130794_bb0015
  article-title: Genetic regulatory mechanisms in the synthesis of proteins
  publication-title: J. Mol. Biol.
  doi: 10.1016/S0022-2836(61)80072-7
– volume: 8
  start-page: 12815
  year: 2018
  ident: 10.1016/j.bbagen.2025.130794_bb0030
  article-title: Excimer based fluorescent pyrene–ferritin conjugate for protein oligomerization studies and imaging in living cells
  publication-title: RSC Adv.
  doi: 10.1039/C8RA00210J
– volume: 11
  year: 2015
  ident: 10.1016/j.bbagen.2025.130794_bb0120
  article-title: Exploring bacterial organelle Interactomes: a model of the protein-protein interaction network in the Pdu microcompartment
  publication-title: PLoS Comput. Biol.
  doi: 10.1371/journal.pcbi.1004067
– volume: 356
  start-page: 1293
  year: 2017
  ident: 10.1016/j.bbagen.2025.130794_bb0090
  article-title: Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell
  publication-title: Science
  doi: 10.1126/science.aan3289
– volume: 19
  year: 2023
  ident: 10.1016/j.bbagen.2025.130794_bb0095
  article-title: Inferring assembly-curving trends of bacterial micro-compartment shell hexamers from crystal structure arrangements
  publication-title: PLoS Comput. Biol.
  doi: 10.1371/journal.pcbi.1011038
– volume: 433
  year: 2021
  ident: 10.1016/j.bbagen.2025.130794_bb0040
  article-title: Self-assembling Shell proteins PduA and PduJ have essential and redundant roles in bacterial microcompartment assembly
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2020.11.020
– volume: 11
  start-page: e03357
  year: 2023
  ident: 10.1016/j.bbagen.2025.130794_bb0085
  article-title: In vitro analysis of bacterial microcompartments and Shell protein superstructures by confocal microscopy, microbiology
  publication-title: Spectrum
– volume: 204
  year: 2022
  ident: 10.1016/j.bbagen.2025.130794_bb0100
  article-title: Linking the Salmonella enterica 1,2-propanediol utilization bacterial microcompartment shell to the enzymatic core via the shell protein PduB
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.00576-21
– volume: 11
  start-page: 4842
  year: 2023
  ident: 10.1016/j.bbagen.2025.130794_bb0070
  article-title: Innate and engineered attributes of bacterial microcompartments for applications in bio-materials science
  publication-title: J. Mater. Chem. B
  doi: 10.1039/D3TB00098B
– volume: 37
  start-page: 9976
  year: 1998
  ident: 10.1016/j.bbagen.2025.130794_bb0060
  article-title: Toward understanding tryptophan fluorescence in proteins
  publication-title: Biochemistry
  doi: 10.1021/bi980274n
– volume: 193
  start-page: 1385
  year: 2011
  ident: 10.1016/j.bbagen.2025.130794_bb0045
  article-title: Genetic analysis of the protein shell of the microcompartments involved in coenzyme B12-dependent 1,2-propanediol degradation by Salmonella
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.01473-10
– volume: 14
  year: 2018
  ident: 10.1016/j.bbagen.2025.130794_bb0080
  article-title: A generic self-assembly process in microcompartments and synthetic protein nanotubes
  publication-title: Small
– volume: 5
  start-page: 252
  year: 2015
  ident: 10.1016/j.bbagen.2025.130794_bb0115
  article-title: Footprints of optimal protein assembly strategies in the operonic structure of prokaryotes
  publication-title: Metabolites
  doi: 10.3390/metabo5020252
– volume: 2
  start-page: 57
  year: 2004
  ident: 10.1016/j.bbagen.2025.130794_bb0010
  article-title: The regulation of bacterial transcription initiation
  publication-title: Nat. Rev. Microbiol.
  doi: 10.1038/nrmicro787
– volume: 29
  start-page: 1727
  year: 1960
  ident: 10.1016/j.bbagen.2025.130794_bb0005
  article-title: The operon: a group of genes whose expression is coordinated by an operator
  publication-title: J. Bacteriol.
– volume: 47
  start-page: 765
  year: 2019
  ident: 10.1016/j.bbagen.2025.130794_bb0105
  article-title: Bio-engineering of bacterial microcompartments: a mini review
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST20170564
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Snippet Operons, clusters of genes under a single promoter, often exhibit a specific gene order influencing their physiological function. While functional relatedness...
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SubjectTerms Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Computational Biology - methods
Escherichia coli - genetics
Escherichia coli - metabolism
FRET
Operon - genetics
Operonic arrangement
Protein Interaction Mapping
Protein Interaction Maps
Protein-protein interactions
Self-assembly
Title Protein-protein interactions as determinants of operon architecture
URI https://dx.doi.org/10.1016/j.bbagen.2025.130794
https://www.ncbi.nlm.nih.gov/pubmed/40086768
https://www.proquest.com/docview/3177481494
Volume 1869
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