Begoña Monterroso Marco

Macromolecular crowding, phase separation and homeostasis in the orchestration of bacterial cellular functions
B. Monterroso, W. Margolin, A.J. Boersma, G. Rivas, B. Poolman, S. Zorrilla
Chemical Reviews (2024)   (doi: 10.1021/acs.chemrev.3c00622)

Benzodioxane-benzamides as promising inhibitors of Escherichia coli FtsZ
L. Suigo, B. Monterroso, M. Sobrinos-Sanguino, C. Alfonso, V. Straniero, G. Rivas, S. Zorrilla, E. Valoti, W. Margolin
Int J Biol Macromol (2023) 253, 126398   (doi: 10.1016/j.ijbiomac.2023.126398)

Bacterial division ring stabilizing ZapA versus destabilizing SlmA modulate FtsZ switching between biomolecular condensates and polymers
B. Monterroso, M.Á. Robles-Ramos, M. Sobrinos-Sanguino, J.R. Luque-Ortega, C. Alfonso, W. Margolin, G. Rivas, S. Zorrilla
Open Biology (2023)13, 220324   (doi: 10.1098/rsob.220324)

The Uso1 globular head interacts with SNAREs to maintain viability even in the absence of the coiled-coil domain
I. Bravo-Plaza, V. G. Tagua, H. N. Arst, Jr, A. Alonso, M. Pinar, B. Monterroso, A. Galindo, M. Á. Peñalva
eLife (2023) 12: e85079  (doi: 10.7554/eLife.85079)

Lipid surfaces and glutamate anions enhance formation of dynamic biomolecular condensates containing bacterial cell division protein FtsZ and its DNA-bound regulator SlmA
G. Paccione, M.A. Robles-Ramos, C. Alfonso, M. Sobrinos-Sanguino, W. Margolin, S. Zorrilla, B. Monterroso, G. Rivas
Biochemistry (2022) 61, 2482   (doi: 10.1021/acs.biochem.2c00424)

FtsZ interactions and biomolecular condensates as potential targets for new antibiotics
S. Zorrilla, B. Monterroso, M.A. Robles-Ramos, W. Margolin, G. Rivas
Antibiotics (2021) 10, 254   (doi: 10.3390/antibiotics10030254)

Assembly of bacterial cell division protein FtsZ into dynamic biomolecular condensates
M.A. Robles-Ramos, S. Zorrilla, C. Alfonso, W. Margolin, G. Rivas, B. Monterroso
BBA-Molecular Cell Research (2021)1868, 118986  (doi: 10.1016/j.bbamcr.2021.118986)

Reconstituting bacterial cell division assemblies in crowded, phase-separated media
B. Monterroso, M.A. Robles-Ramos, S. Zorrilla, G. Rivas
In Methods in Enzymology: Liquid-Liquid Phase Coexistence and Membraneless Organelles (2021) 646, 19-49  (doi: 10.1016/bs.mie.2020.06.012)

The nucleoid occlusion protein SlmA binds to lipid membranes
M.A. Robles-Ramos, W. Margolin, M. Sobrinos-Sanguino, C. Alfonso, G. Rivas, B. Monterroso, S. Zorrilla
mBio (2020) 11, e02094-20   (doi: 10.1128/mBio.02094-20)

The bacterial DNA binding protein MatP involved in linking the nucleoid terminal domain to the divisome at midcell interacts with lipid membranes
B. Monterroso, S. Zorrilla, M. Sobrinos-Sanguino, M. Robles-Ramos, C. Alfonso, B. Söderström, N. Meiresonne, J. Verheul, T. den Blaauwen, G. Rivas
mBio (2019) 10, e00376-19  (doi: 10.1128/mBio.00376-19)

Bacterial FtsZ protein forms phase-separated condensates with its nucleoid-associated inhibitor SlmA
B. Monterroso, S. Zorrilla, M. Sobrinos-Sanguino, M.A. Robles-Ramos, M. López-Álvarez, W. Margolin, C.D. Keating, G. Rivas
EMBO R. (2019) 20, e45946  (doi: 10.15252/embr.201845946)
Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads
M. Sobrinos-Sanguino, S. Zorrilla, B. Monterroso, A.P. Minton, G. Rivas
Sci. Rep. (2017) 7, 13707  (doi: 10.1038/s41598-017-14160-y)

Encapsulation of compartmentalized cytoplasm mimic within lipid membrane by microfluidics
M. Sobrinos-Sanguino, S. Zorrilla, C.D. Keating, B. Monterroso, G. Rivas
Chem Commun. (2017) 53, 4775-4778   (doi: 10.1039/C7CC01289F)

Microenvironments created by liquid-liquid phase transition control the dynamic distribution of bacterial division FtsZ protein
B. Monterroso, S. Zorrilla, M. Sobrinos-Sanguino, C.D. Keating, G. Rivas
Sci. Rep. (2016) 6, 35140   (doi: 10.1038/srep35140)

Charged molecules modulate the volume exclusion effects exerted by crowders on FtsZ polymerization
B. Monterroso, B. Reija, M. Jiménez, S. Zorrilla, G. Rivas
PLoS ONE (2016) 11, e0149060  (doi: 10.1371/journal.pone.0149060)

The nucleoid occlusion SlmA protein accelerates the disassembly of the FtsZ protein polymers without affecting their GTPase activity
E.J. Cabré, B. Monterroso, C. Alfonso, A. Sánchez-Gorostiaga, B. Reija, M. Jiménez, M. Vicente, S. Zorrilla, G. Rivas
PLoS ONE (2015) 10, e0126434  (doi: 10.1371/journal.pone.0126434)

A new calmodulin-binding motif for inositol 1,4,5-trisphosphate 3-kinase regulation
E. Franco-Echevarría, J. I. Baños-Sanz, B. Monterroso, A. Round, J. Sanz-Aparicio, B. González
Biochem. J. (2014) 463, 319-328   (doi: 10.1042/BJ20140757)

Control by potassium of the size-distribution of Escherichia coli FtsZ polymers is independent of GTPase activity
R. Ahijado-Guzmán, C. Alfonso, B. Reija, E. Salvarelli, J. Mingorance, S. Zorrilla, B. Monterroso, G. Rivas
J. Biol. Chem. (2013) 288, 27358-27365   (doi: 10.1074/jbc.M113.482943)

MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunits
V. Hernández-Rocamora, C. García-Montañés, B. Reija, B. Monterroso, W. Margolin, C. Alfonso, S. Zorrilla, G. Rivas
J. Biol. Chem. (2013) 288, 24625-24635   (doi: 10.1074/jbc.M113.483222)

Combined analytical ultracentrifugation, light scattering and fluorescence spectroscopy studies on the functional associations of the bacterial division FtsZ protein
B. Monterroso, C. Alfonso, S. Zorrilla, G. Rivas
Methods (2013) 59, 349-362   (doi: 10.1016/j.ymeth.2012.12.014)

Self-organization of the bacterial cell-division protein FtsZ in confined environments
S. Mellouli, B. Monterroso, R. Vutukuri, E. Brinke, V. Chokkalingam, G. Rivas, W. T. S. Huck
Soft Matter (2013) 9, 10493-10500   (doi: 10.1039/C3SM51163D)

Macromolecular interactions of the bacterial division FtsZ protein: from quantitative biochemistry and crowding to reconstructing minimal divisomes in the test tube
G. Rivas, C. Alfonso, M. Jiménez, B. Monterroso, S. Zorrilla
Biophys. Rev. (2013) 5, 63-77   (doi: 10.1007/s12551-013-0115-1)

An equilibrium model for the Mg2+-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue
B. Monterroso, G. Rivas, A.P. Minton
Biochemistry (2012) 51, 6108-6113   (doi: 10.1021/bi300891q)

Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli
A. Martos, B. Monterroso, S. Zorrilla, B. Reija, C. Alfonso, J. Mingorance, G. Rivas, M. Jiménez
PLoS ONE (2012) 7, e39829  (doi: 10.1371/journal.pone.0039829)

Mg2+-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue involves the concerted formation of a narrow size distribution of oligomeric species
B. Monterroso, R. Ahijado-Guzmán, B. Reija, C. Alfonso, S. Zorrilla, A.P. Minton, G. Rivas
Biochemistry (2012) 51, 4541-4550   (doi: 10.1021/bi300401b)

Development of a Homogeneous Fluorescence Anisotropy Assay to Monitor and Measure FtsZ Assembly in solution
B. Reija, B. Monterroso, M. Jiménez, M. Vicente, G. Rivas, S. Zorrilla
Anal Biochem. (2011) 418, 89-96   (doi: 10.1016/j.ab.2011.07.001)

The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis
R.P. McGlinchey, F. Shewmaker, P. McPhie, B. Monterroso, K. Thurber, R.B. Wickner
Proc. Natl. Acad. Sci. USA. (2009) 106, 13731-13736   (doi: 10.1073/pnas.0906509106)

Insights into the structure-function relationship of pneumococcal cell wall lysozymes, LytC and Cpl-1
B. Monterroso, J.L. Sáiz, P. García, J.L. García, M. Menéndez
J. Biol. Chem. (2008) 283, 28618-28628   (doi: 10.1074/jbc.M802808200)

Effect of high concentration of “inert” cosolutes on the refolding of an enzyme: Carbonic Anhydrase B in sucrose and Ficoll 70
B. Monterroso, A.P. Minton
J. Biol. Chem. (2007) 282, 33452-33458   (doi: 10.1074/jbc.M705157200)

Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage Endolysin Cpl-1
I. Pérez-Dorado, N. Campillo, B. Monterroso, D. Hesek, M. Lee, J.A. Páez, P. García, M. Martínez-Ripoll, J.L. García, S. Mobashery, M. Menéndez, J.A. Hermoso
J. Biol. Chem. (2007) 282, 24990-24999  (doi: 10.1074/jbc.M704317200)

Insights into molecular plasticity of choline binding proteins (Pneumococcal surface proteins) by SAXS
R.M. Buey, B. Monterroso, M. Menéndez, G. Diakun, P. Chacón, J.A. Hermoso, J.F. Díaz
J. Mol. Biol. (2007) 365, 411-424  (doi: 10.1016/j.jmb.2006.09.091)

Unravelling the structure of the pneumococcal autolytic lysozyme
B. Monterroso, C. López-Zumel, J.L. García, J.L. Sáiz, P. García, N. Campillo, M. Menéndez
Biochem. J. (2005) 391, 41-49   (doi: 10.1042/BJ20050612)

Structural and thermodynamic characterization of Pal, a phage natural chimeric lysin active against Pneumococci
J. Varea, B. Monterroso, J.L. Sáiz, C. López-Zumel, J.L. García, J. Laynez, P. García, M. Menéndez
J. Biol. Chem. (2004) 279, 43697-43707  (doi: 10.1074/jbc.M407067200)

pH effect on cysteine and cystine behavior at hanging drop mercury electrode
B. Monterroso-Marco, B. López Ruiz
Talanta (2003) 61, 733-741  (doi: 10.1016/S0039-9140(03)00336-9)

Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1
J. Hermoso, B. Monterroso, A. Albert, B. Galán, O. Ahrazem, P. García, M. Martínez-Ripoll, J.L. García, M. Menéndez
Structure (2003) 11, 1239-1249  (doi: 10.1016/j.str.2003.09.005)

Crystallization and preliminary X-ray diffraction studies of the complete modular endolysin from Cp-1, a phage infecting Streptococcus pneumoniae
B. Monterroso, A. Albert, M. Martínez-Ripoll, P. García, J.L. García, M. Menéndez, J. Hermoso
Acta Cryst. (2002) D58 1487-1489  (doi: 10.1107/S0907444902011563)

Characterization of Ejl, the cell-wall amidase coded by the pneumococcal bacteriophage Ej-1
J.L. Sáiz, C. López-Zumel, B. Monterroso, J. Varea, J.L.R. Arrondo, I. Iloro, J.L. García, J. Laynez, M. Menéndez
Protein Sci. (2002) 11, 1788-1799  (doi: 10.1110/ps.4680102)

Do Sequence Repeats Play an Equivalent Role in the Choline-binding Module of Pneumococcal LytA Amidase?
J. Varea, J.L. Sáiz, C. López-Zumel, B. Monterroso, F.J. Medrano, J.L.R. Arrondo, I. Iloro, J. Laynez, J.L. García, M. Menéndez
J. Biol. Chem. (2000) 275, 26842-26855  (doi: 10.1016/S0021-9258(19)61452-3)