Author

K. Rajasekar

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 3 Organism:E. coli· 3 Approach:experimental assay· 3 Research Focus:chromatin & epigenetic regulation· 2 Approach:wet-lab / biochemical assay· 2 Research Focus:cell type annotation· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

r. baker· 2 shared C. Kleanthous· 1 shared C. Redfield· 1 shared C. V. Robinson· 1 shared D. J. Sherratt· 1 shared D. Sherratt· 1 shared F. Samsudin· 1 shared G. Fisher· 1 shared

Activity by Year

2017-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersBiochemistry

r. baker

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Author profile →

3 papers

Recent·Most cited

Competitive binding of MatP and topoisomerase IV to the MukB dimerization hinge

G. Fisher, J. R. Bolla, K. Rajasekar, j. makela, r. baker, m. zhou, j. prince, M. Stracy, C. V. Robinson, L. K. Arciszewska, D. Sherratt

The paper shows MatP and topoisomerase IV ParC compete for binding to the MukB dimerization hinge, with matS binding displacing MatP from the hinge.

bioRxiv · Mar 3, 2021 · PreprintBiochemistry

Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism

J. Szczepaniak, P. Holmes, K. Rajasekar, R. Kaminska, F. Samsudin, P. G. Inns, P. Rassam, S. Khalid, S. M. Murray, C. Redfield, C. Kleanthous

The paper shows the Tol system in E. coli actively mobilizes and captures Pal to coordinate outer membrane constriction with cell division.

bioRxiv · Oct 4, 2019 · PreprintMicrobiology

Asymmetric MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin

K. Zawadzka, P. Zawadzki, R. Baker, K. Rajasekar, D. J. Sherratt, L. Arciszewska

The paper shows that MukF's N- and C-terminal domains independently regulate the two MukB ATPases in the MukBEF complex, forming an asymmetric tripartite structure during ATP cycles.

bioRxiv · Aug 25, 2017Biochemistry