Staff Profile
Dr Victor Hernandez-Rocamora
Research Associate
- Telephone: (0)191 2083211
- Address: Biosciences Institute
The Centre for Bacterial Cell Biology
Room 2.05, Baddiley-Clark Building
Medical School
Newcastle University
Richardson Road
Newcastle upon Tyne
NE2 4AX
United Kingdom
Background
I am a Research Associate in the Centre for Bacterial Cell Biology in Newcastle University since 2014 and I am part of the group of Waldemar Vollmer. Here I study the proteins involved in the metabolism of peptidoglycan in bacteria using a biophysical approach with a focus on the membrane-associated steps of peptidoglcyan synthesis.
Before, I worked as a post-doc in the Centro de Investigaciones Biológicas (CSIC) in Madrid (Spain) from 2009 until 2014. My group leader was German Rivas. In his group, I used biophysical and biochemical methods to study cell division in Escherichia coli. I was involved in studying the interaction between membrane proteins reconstitued in nanodiscs and soluble components of the cell division ring. I also studied inhibitors of FtsZ polymerisation such as MinC and the Kil peptide from the lambda phage using biophisical methods.
I obtained my PhD in Instituto de Biología Molecular y Celular in Universidad Miguel Hernández in Elche (Spain), from 2004 to 2009. The title of my thesis was “Structural and functional study of proteins of biotechnological interest. Applications and optimization”. My thesis supervisor was Jesus M. Sanz. On the one hand, I used protein engineering of the choline-biding domain of LytA from Streptococcus pneumoniae in order to develop new biotechnological applications. On the other hand, I was involved in the structural and biophysical study of PaaX, a transcriptional regulator for the catabolism of phenylacetic acid in Escherichia coli.
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Publications
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Articles
- Alodaini D, Hernandez-Rocamora V, Boelter G, Ma X, Alao MB, Doherty HM, Bryant JA, Moynihan P, Moradigaravand D, Glinkowska M, Vollmer W, Banzhaf M. Reduced peptidoglycan synthesis capacity impairs growth of E. coli at high salt concentration. mBio 2024, 15(4), e00325-24.
- Oluwole AO, Hernandez-Rocamora VM, Cao Y, Li X, Vollmer W, Robinson CV, Bolla JR. Real-Time Biosynthetic Reaction Monitoring Informs the Mechanism of Action of Antibiotics. Journal of the American Chemical Society 2024, 146(10), 7007–7017.
- Wang H-J, Hernandez-Rocamora VM, Kuo C-I, Hsieh K-Y, Lee S-H, Ho M-R, Tu Z, Vollmer W, Chang C-I. Structural basis for the hydrolytic activity of the transpeptidase-like protein DpaA to detach Braun’s lipoprotein from peptidoglycan. mBio 2023, 14(5), e01379-23.
- Xu Y, Hernandez-Rocamora VM, Lorent J, Cox R, Wang X, Bao X, Stel M, Vos G, vandenBos R, Pieters R, Gray J, Vollmer W, Breukink E. Metabolic labeling of the bacterial peptidoglycan by functionalized glucosamine. iScience 2022, 25(8), 104753.
- Hernández-Rocamora VM, Baranova N, Peters K, Breukink E, Loose M, Vollmer W. Real-time monitoring of peptidoglycan synthesis by class A PBPs on the membrane. eLife 2021, 10, e61525.
- Winkle M, Hernández-Rocamora VM, Pullela K, Goodall ECA, Martorana AM, Gray J, Henderson IR, Polissi A, Vollmer W. DpaA Detaches Braun’s Lipoprotein from Peptidoglycan. mBio 2021, 12(3), e00836-21.
- Baranova N, Radler P, Hernandez-Rocamora V, Alfonso C, Lopez-Pelegrin MDM, Rivas G, Vollmer W, Loose M. Diffusion and capture permits dynamic coupling between treadmilling FtsZ filaments and cell division proteins. Nature Microbiology 2020, 5, 407-417.
- Hernández-Rocamora VM, Otten CF, Radkov A, Simorre JP, Breukink E, Van Nieuwenhze M, Vollmer W. Coupling of polymerase and carrier lipid phosphatase prevents product inhibition in peptidoglycan synthesis. The Cell Surface 2018, 2, 1-13.
- Hernandez-Rocamora VM, Alfonso C, Margolin W, Zorrilla S, Rivas G. Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits. Journal of Biological Chemistry 2015, 290(33), 20325-20335.
- Hernandez-Rocamora VM, Garcia-Montanes C, Rivas G. Phospholipid bilayer nanodiscs: A powerful tool to study the structural organization and biochemical reactivity of proteins in membrane-like environments. Current Topics in Medicinal Chemistry 2014, 14(23), 2637-2646.