rod shaped

Edge evidence

• MreB enables Rod complex RO:0002327

  MreB organizes rod-shape elongation machinery.

  • DOI:10.1146/annurev-cellbio-010521-010834 MreB filaments interact with Rod complexes Supports MreB-Rod complex interaction in rod-shape regulation.
• Rod complex directs peptidoglycan synthesis RO:0002211

  Rod complexes direct sidewall peptidoglycan synthesis.

  • DOI:10.1146/annurev-cellbio-010521-010834 Rod complexes drive cell wall insertion Supports Rod complex contribution to wall insertion.
• peptidoglycan synthesis produces lateral cell-wall elongation METPO:2000202

  Directed peptidoglycan synthesis elongates rod-shaped cells.

  • DOI:10.1038/nrmicro2677 elongation mode of peptidoglycan synthesis Supports peptidoglycan synthesis in cell elongation.
• lateral cell-wall elongation regulates rod shaped RO:0002211

  Lateral wall elongation preserves the cylindrical rod morphology.

  • DOI:10.1016/j.tim.2011.11.004 restores its rod shape Supports MreB-associated cell-wall synthesis as important for rod shape restoration and maintenance.
• FtsZ coordinates with peptidoglycan synthesis

  FtsZ coordinates division-associated peptidoglycan synthesis with rod cell morphology.

  • DOI:10.1038/nrmicro1205 FtsZ collaborates with penicillin binding proteins Supports FtsZ-PBP collaboration in bacterial cell-shape generation.
• RodA-PBP2 complex positively regulates rod shaped

  The active elongation synthase complex supports proper rod-shaped morphology during growth.

  • DOI:10.1038/s41467-023-39037-9 Structural opening couples RodA glycan polymerization and PBP2 crosslinking, a coupling essential in vivo for rod-shaped growth.
• PBP2 structural opening activates RodA polymerization activity RO:0002213

  Conformational opening of PBP2 allosterically stimulates RodA polymerization.

  • DOI:10.1038/s41467-023-39037-9 Structural opening promotes RodA polymerization activity.
• PBP2 structural opening enables peptidoglycan crosslinking RO:0002327

  The open state elevates the PBP2 TP domain toward the PG layer, enabling crosslinking.

  • DOI:10.1038/s41467-023-39037-9 Opening of PBP2 elevates the TP domain, facilitating crosslinking.
• MreC activates RodA-PBP2 complex RO:0002213

  MreC binds the PBP2 pedestal domain and biases RodA-PBP2 into the open, catalytically active conformation.

  • DOI:10.1038/s41467-023-39037-9 MreC is implicated as an activator that promotes the open, catalytically active conformation of PBP2.
• RodA polymerization activity regulates elongasome processivity RO:0002211

  RodA abundance/activity tunes processive dynamics of MreB-associated elongasomes.

  • DOI:10.1038/s41467-024-49785-x RodA abundance regulates elongasome processivity, reversal frequency, and pausing.
• elongasome processivity contributes to rod-shaped sidewall reinforcement RO:0002326

  Processive circumferential synthesis lays long glycan hoops that mechanically reinforce the cylinder.

  • DOI:10.1038/s41467-024-49785-x Long glycan strands act as barrel-hoop-like reinforcing structures of the rod sidewall.