The prevalent DNA modification in eukaryotes is C5-cytosine methylation. Biophysically, this modification stabilizes double-stranded DNA. Evolution has built on and enhanced this tendency to utilize C5-methylation, which predominantly occurs in the symmetric CpG context for transcription control. Consistent with its biophysical effects, methylation in transcription control structures (e.g., promoters) represses transcription; methylation elsewhere (e.g., gene bodies) enhances transcription by suppressing aberrant initiation. Methylation can be introduced in one step by de novo and maintenance methyltransferases and propagated by feed-forward loops that link DNA methylation and repressive chromatin marks. Methylation is most easily lost passively as a result of DNA replication, but it can also be actively erased through a mechanism that utilizes TET catalyzed oxidation to prime DNA for base excision repair. The genetics and cell biology of DNA methylation are unique to eukaryotes, but the biochemistry of DNA methylation (and to some extent also DNA demethylation) is also conserved in prokaryotes. We seek to answer biochemical questions using more robust bacterial proteins and answer genetic/ cell biological questions using zebrafish models and human genetic data (e.g., for malignancies with defects in demethylation machinery).


In 2019, we continued our research on relatively well-behaved prokaryotic model proteins to study the specific recognition of 5-methylcytosine and its oxidized congeners in DNA. The repertoire of 5mC and 5hmC binding proteins is relatively small, and most proteins that specifically bind DNA with these bases contain the same domains. Domains that bind fully methylated DNA in the context of CpG include zinc finger and MBD domains. In contrast, hemi-methylated DNA is typically bound by SRA domains. During the last year, we considerably broadened the repertoire of known domains that recognize 5mC and 5hmC. SRA domains belong to the larger superfamily of PUA domains, which also comprises PUA domains in the strict sense, ASCH domains, EVE domains, and several other lesser known domain groups. To the extent that function was known, a clear division of labor appeared to be in place. SRA domains were associated with the binding of modified DNA, whereas other families within the PUA superfamily either were known to be involved in the binding or processing of modified RNA or had completely unknown functions. In silico screens that were performed in collaboration with Dr. Shuang-Yong Xu (New England Biolabs) showed that many PUA superfamily domains in bacteria are fused to endonucleolytic domains that are associated with DNA cleavage. Subsequent biochemical experiments demonstrated that the fusion proteins indeed cleaved modified DNA, although not with the same degree of specificity as SRA domains (Lutz et al., Nucleic Acids Res, 2019). We also crystallographically characterized a few prototype enzymes and solved their structures with and without DNA. The structures illustrate the mode of recognition of methyl- or hydroxymethyl modifications. Similar DNA modification-sensing domains exist in eukaryotes and have been implicated in malignancies, but their biochemical behavior requires further investigation. NEco is the modification-sensing domain of EcoKMcrA, which is one of the earliest studied restriction endonucleases of E. coli. EcoKMcrA efficiently restricts DNA that contains 5mC or 5hmC, provided the modifications are present in the right context. Efficiency is much greater for fully methylated DNA than for hemi-methylated DNA. Our previous work indicated that the NEco modification-sensing domain was phylogenetically unrelated to other methylationsensing domains. In 2019, we elucidated the binding mode of the domain to modified DNA and found that modification sensing is also locally very different from previous observations (Slyvka et al., Nucleic Acids Res, 2019). To date, NEco has been shown to be very good at discriminating (hydroxy)methylated from unmethylated DNA. Further research will likely expand the currently known and narrowly defined phylogenetic distribution (Fig. 1).


fig.1. Modification-dependent DNA binding by the N-terminal domain of EcoKMcrA endonuclease (NEco). (Top) Interaction between fully modified DNA with (hydroxy)methyl binding pockets of EcoKMcrA. (Bottom) Sequence and modification specificity of EcoKMcrA N-terminal domain determined by EMSA competition experiments (for experimental details, see Slyvka et al., Nucleic Acids Res, 2019).


In contrast to methylation sensing, demethylation has no clear equivalent in prokaryotes and thus needs to be studied using eukaryotic models. Our research primarily focuses on the ways in which TET proteins identify their targets. Two of our collaborators, Dr. Tomasz Jurkowski (Cardiff University, United Kingdom) and Dr. Tim Hore (Otago University, New Zealand), provided strong biochemical evidence that the locus specificity of TETs is at least partially attributable to sequence specificity. We solved structures with preferred and discriminated substrates to better understand the mode of sequence recognition. Based on the lack of sequence-specific contacts between TETs and their target DNAs outside the CpG core recognition sequence, we initially hypothesized that DNA bending was responsible for sequence specificity. Our crystal structures do not support this hypothesis, however, and instead reveal an unexpected mechanism of sequence recognition that also explains similarities in preference of different TET paralogues. We are also continuing our work on links between DNA reprogramming and DNA repair. Some of our experiments, such as investigating the role of NEIL1 and TDG in the excision of oxidized 5-methylcytosine bases, are consistent with the general paradigm that DNA reprogramming co-opts DNA repair. However, based on much circumstantial evidence and the work of others, we suspect that the converse may also be true and that DNA repair may use intermediates that are normally associated with reprogramming. We will test this hypothesis both biochemically and bioinformatically.


 bochtler m

Matthias Bochtler, PhD, Professor 

Correspondence address:
Laboratory of Structural Biology
International Institute of Molecular and Cell Biology
4 Ks. Trojdena Street, 02-109 Warsaw, Poland
Email: This email address is being protected from spambots. You need JavaScript enabled to view it.
Office: This email address is being protected from spambots. You need JavaScript enabled to view it.
tel: +48 (22) 597 0732; fax: +48 (22) 597 0715


2009 - Professor of Biological Sciences, nomination by the President of the Republic of Poland

2006 - DSc Habil, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznań, Poland

1999 - PhD in Biochemistry, Technical University of Munich, Germany

1995 - MSc in Experimental Physics, Munich University, Germany


2011-present - Professor, Head of Laboratory of Structural in Biology, International Institute of Molecular and Cell Biology in Warsaw, Poland, and Laboratory of Genome Engineering, Institute of Biochemistry and Biophysics, Polish Academy of Sciences,Warsaw, Poland

2007-2011 - Part-time Director of Structural Biology, Cardiff University, United Kingdom

2001-2010 - Head, Joint MPG-PAS Junior Research Group, International Institute of Molecular and Cell Biology in Warsaw, Poland

2000 - Patent training, Weickmann & Weickmann

1999-2000 - Postdoctoral Fellow, Max Planck Institute of Biochemistry, Martinsried, Germany


1996-1999 - Research Assistant, Max Planck Institute of Biochemistry, Martinsried, Germany

1995-1996 - Internship, Medical Microbiology, University of Regensburg,  Germany

1992-1993 - Guest Student, Cambridge University, United Kingdom

1990-1992 - Studies in Physics, Munich University, Germany


2018 - TEAM Foundation for Polish Science

2018 - International Academic Partnerships Programme, Polish National Agency for Academic Exchange

2018 - DAINA, National Science Centre

2015 - HARMONIA, National Science Centre

2012 - MAESTRO, National Science Centre

2011 - TEAM, Foundation for Polish Science Professor Stefan Pieńkowski Award

2004 - EMBO/HHMI Young Investigator Award

2000 - Crystal Award, Germany

1998 - Crystal Award Germany

1990 – 1992 - Scholarship from Deutsche Studienstiftung and Bavarian State


R. Filipek, M. Firczuk, M. Lipka, R. Szczepanowski, M. Kaus-Drobek, M. Sokołowska, G. Chojnowski, H. Korza, M. Wojciechowski, W. Siwek, P. Haniewicz, A.A. Kazrani, K. Mierzejewska.

bochtler lab

Lab Leader:

  • Matthias Bochtler, PhD, Professor

Senior Researcher:

  • Honorata Czapińska, PhD, DSc Habil

Postdoctoral Researchers:

  • Marek Wojciechowski, PhD

PhD Students:

  • Igor Helbrecht, MSc

  • Magdalena Klimczak, MSc

  • Norbert Osiński, MSc

  • Michał Pastor, MSc

  • Abhishek Pateria, MSc

  • Dominik Rafalski, MSc

  • Anton Slyvka, MSc

  • Anna Stroynowska-Czerwińska, MSc

  • Katarzyna Krakowska, MSc

Another co-worker:

  • Anna Fedenko, MSc

Lab Technician:

  • Agnieszka Olszewska (part-time)

Laboratory Support Specialist:

  • Aleksandra Jakielaszek, MSc Eng.



This email address is being protected from spambots. You need JavaScript enabled to view it.


The Nε-rule for serine, but not cysteine catalytic triads.

Czapińska H, Bochtler M.

Angew Chem Int Ed Engl.. 2022

Adar-mediated A-to-I editing is required for embryonic patterning and innate immune response regulation in zebrafish.

Niescierowicz K#, Pryszcz L#, Navarrete C#, Tralle E#, Sulej A#, Abu Nahia K, Kasprzyk ME, Misztal K, Pateria A, Pakuła A, Bochtler M, Winata C.

# Contributed equally

Nat Commun.. 2022

Pronounced sequence specificity of the TET enzyme catalytic domain guides its cellular function.

Ravichandran M, Rafalski D, Davies CI, Ortega-Recalde O, Nan X, Glanfield CR, Kotter A, Misztal K, Wang AH, Wojciechowski M, Rażew M, Mayyas IM, Kardailsky O, Schwartz U, Zembrzycki K, Morison IM, Helm M, Weichenhan D, Jurkowska RZ, Krueger F, Plass C, Zacharias M, Bochtler M, Hore TA, Jurkowski TP.

Sci Adv.. 2022

Prevalence and risk factors of untreated thyroid dysfunctions in the older Caucasian adults: Results of PolSenior 2 survey.

Kocełak P, Mossakowska M, Puzianowska-Kuźnicka M, Sworczak K, Wyszomirski A, Handzlik G, Stefański A, Zdrojewski T, Chudek J.

PLoS One. 2022

Competition between electrostatic interactions and halogen bonding in the protein–ligand system: structural and thermodynamic studies of 5,6-dibromobenzotriazole-hCK2α complexes.

Winiewska‑Szajewska M, Czapinska H, Kaus‑Drobek M, Fricke A, Mieczkowska K, Dadlez M, Bochtler M, Poznański J.

Sci Rep.. 2022


DNA adenine methylation in eukaryotes: Enzymatic mark or a form of DNA damage?

Bochtler M, Fernandes H.

BioEssays. 2021

Crystal structures of the EVE-HNH endonuclease VcaM4I in the presence and absence of DNA.

Pastor M, Czapinska H, Helbrecht I, Krakowska K, Lutz T, Xu S, Bochtler M.

Nucleic Acids Res.. 2021

Halogen Atoms in the Protein-Ligand System. Structural and Thermodynamic Studies of the Binding of Bromobenzotriazoles by the Catalytic Subunit of Human Protein Kinase CK2.

Czapinska H, Winiewska-Szajewska M, Szymaniec-Rutkowska A, Piasecka A, Bochtler M, Poznański J.

J Phys Chem B.. 2021

Distinction between self and non-self in restriction modification: The mysterious case of type IIL enzymes.

Bochtler M.

Structure. 2021


Arrhenius-law-governed homo- and heteroduplex dissociation.

Bochtler M.

Phys Rev E. 2020

In Vitro Directed Evolution of a Restriction Endonuclease With More Stringent Specificity.

Skowronek KJ, Bochtler M.

J Vis Exp . 2020

Restriction endonucleases that cleave RNA/DNAheteroduplexes bind dsDNA in A-like conformation.

Kisiala M, Kowalska M, Pastor M, Korza HJ, Czapinska H, Bochtler M.

Nucleic Acids Res.. 2020

Protein Domain Guided Screen for Sequence Specific and Phosphorothioate-Dependent Restriction Endonucleases.

Lutz T, Czapinska H, Fomenkov A, Potapov V, Heiter DF, Cao B, Dedon P, Bochtler M, Xu S.

Front. Microbiol.. 2020

Targeted RNA Knockdown by a Type III CRISPR-Cas Complex in Zebrafish.

Fricke T, Smalakyte D, Lapinski M, Pateria A, Weige C, Pastor M, Kolano A, Winata C, Siksnys V, Tamulaitis G, Bochtler M.

CRISPR J.. 2020

Reversal of nucleobase methylation by dioxygenases.

Xu G-L, Bochtler M.

Nat Chem Biol. 2020


Structural bases of peptidoglycan recognition by lysostaphin SH3b domain.

Mitkowski P, Jagielska E, Nowak E, Bujnicki JM, Stefaniak F, Niedziałek D, Bochtler M, Sabała I.

Sci Rep.. 2019

Crystal Structure and Directed Evolution of Specificity of NlaIV Restriction Endonuclease.

Czapinska H, Siwek W, Szczepanowski RH, Bujnicki JM, Bochtler M, Skowronek KJ.

J Mol Biol.. 2019

A protein architecture guided screen for modification dependent restriction endonucleases.

Lutz T, Flodman K, Copelas A, Czapinska H, Mabuchi M, Fomenkov A, He X, Bochtler M, Xu S.

Nucleic Acids Res.. 2019

Crystal structure of the EcoKMcrA N-terminal domain (NEco): recognition of modified cytosine bases without flipping.

Slyvka A, Zagorskaitė E, Czapinska H, Sasnauskas G, Bochtler M.

Nucleic Acids Res.. 2019


Activity and structure of EcoKMcrA.

Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M.

Nucleic Acids Res.. 2018

Crystal structure of the modification-dependent SRA-HNH endonuclease TagI

Kisiala M, Copelas A, Czapinska H, Xu S, Bochtler M.

Nucleic Acids Res.. 2018

Crystal structure of human Acinus RNA recognition motif domain.

Fernandes H, Czapinska H, Grudziaz K, Bujnicki JM, Nowacka M.

PeerJ.. 2018

Specificity of MLL1 and TET3 CXXC domains towards naturally occurring cytosine modifications.

Stroynowska-Czerwinska A, Piasecka A, Bochtler M.

Biochim Biophys Acta Gene Regul Mech.. 2018

Unique mechanism of target recognition by PfoI restriction endonuclease of the CCGG-family.

Tamulaitiene G, Manakova E, Jovaisaite V, Tamulaitis G, Grazulis S, Bochtler M, Siksnys V.

Nucleic Acids Res.. 2018

The Bacteroidetes Q-Rule: Pyroglutamate in Signal Peptidase I Substrates.

Bochtler M, Mizgalska D, Veillard F, Nowak ML, Houston J, Veith P, Reynolds EC, Potempa J.

Front Microbiol.. 2018

Shifting meiotic to mitotic spindle assembly in oocytes disrupts chromosome alignment.

Bennabi I, Quéguiner I, Kolano A, Boudier T, Mailly P, Verlhac MH, Terret ME.

EMBO Rep.. 2018

The Y. bercovieri Anbu crystal structure sheds light on the evolution of highly (pseudo)symmetric multimers.

Piasecka A, Czapinska H, Vielberg MT, Szczepanowski RH, Kiefersauer R, Reed S, Groll M, Bochtler M.

J Mol Biol.. 2018


A TALE-inspired computational screen for proteins that contain approximate tandem repeats.

Perycz M, Krwawicz J, Bochtler M.

PLoS One. 2017

Nei-like 1 (NEIL1) excises 5-carboxylcytosine directly and stimulates TDG-mediated 5-formyl and 5-carboxylcytosine excision.

Slyvka A, Mierzejewska K, Bochtler M.

Sci Rep.. 2017


Isolation of Plant Photosystem II Complexes by Fractional Solubilization

Haniewicz P, Floris D, Farci D, Kirkpatrick J, Loi MC, Büchel C, Bochtler M, Piano D

Front Plant Sci. 2016

On the role of steric clashes in methylation control of restriction endonuclease activity

Mierzejewska K, Bochtler M, Czapinska H

Nucleic Acids Res. 2016

Haloferax volcanii UbaA, catalytic engine for sampylation and sulfur transfer

Bochtler M., Piasecka A

FEBS J. 2016

Type III CRISPR complexes from Thermus thermophilus

Szychowska M, Siwek W, Pawolski D, Kazrani AA, Pyrc K, Bochtler M

Acta Biochim Pol. 2016

DNA demethylation pathways: Additional players and regulators

Bochtler M, Kolano A, Xu G-L

Bioessays. 2016


Functional Analysis of Porphyromonas gingivalis W83 CRISPR-Cas Systems

Burmistrz M, Dudek B, Staniec D, Rodriguez Martinez JI, Bochtler M, Potempa J, Pyrc K

J Bacteriol. 2015

High resolution structure of an M23 peptidase with a substrate analogue

Grabowska M, Jagielska E, Czapinska H, Bochtler M, Sabala I

Sci Rep. 2015


Carboxy terminus of GATA4 transcription factor is required for its cardiogenic activity and interaction with CDK4

Gallagher JM, Yamak A, Kirilenko P, Black S, Bochtler M, Lefebvre C, Nemer M, Latinkić BV

Mech Dev. 2014

NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme

Jaremko M, Jaremko L, Nowakowski M, Wojciechowski M, Szczepanowski RH, Panecka R, Zhukov I, Bochtler M, Ejchart A

J Struct Biol. 2014

Crystal structure of the 5hmC specific endonuclease PvuRts1I

Kazrani AA, Kowalska M, Czapinska H, Bochtler M

Nucleic Acids Res.. 2014

Insights into DNA hydroxymethylation in the honeybee from in-depth analyses of TET dioxygenase

Wojciechowski M, Rafalski D, Kucharski R, Misztal K, Maleszka J, Bochtler M, Maleszka R

Open Biol. 2014

Structural basis of the methylation specificity of R.DpnI

Mierzejewska K, Siwek W, Czapinska H, Kaus-Drobek M, Radlinska M, Skowronek K, Bujnicki JM, Dadlez M, Bochtler M

Nucleic Acids Res.. 2014

Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans

Sabala I, Jagielska E, Bardelang PT, Czapinska H, Dahms SO, Sharpe JA, James R, Than ME, Thomas NR, Bochtler M

FEBS J. 2014


CpG Underrepresentation and the Bacterial CpG Specific DNA Methyltransferase M.MpeI

Wojciechowski M, Czapinska H, Bochtler M

Proc Natl Acad Sci U S A.. 2013

Isolation of monomeric photosystem II that retains the subunit PsbS

Haniewicz P, De Sanctis D, Büchel C, Schröder WP, Loi MC, Kieselbach T, Bochtler M, Piano D

Photosynth Res. 2013


RIBER/DIBER: a software suite for crystal content analysis in the studies of protein-nucleic acid complexes

Chojnowski G, Bujnicki JM, Bochtler M

Bioinformatics. 2012

Crystal structure and mechanism of action of the N6-methyladenine dependent type IIM restriction endonuclease

Siwek W, Czapinska H, Bochtler M, Bujnicki JM, Skowronek K

Nucleic Acids Res. 2012

Anti-staphylococcal activities of lysostaphin and LytM catalytic domain

Sabala I, Jonsson IM, Tarkowski A, Bochtler M

BMC Microbiol. 2012

Structural basis of the TAL effector-DNA interaction

Bochtler M

Biol Chem. 2012


Hpy188I-DNA pre- and post-cleavage complexes--snapshots of the GIY-YIG nuclease mediated catalysis

Sokolowska M, Czapinska H, Bochtler M

Nucleic Acids Res. 2011

Amyloid-associated nucleic acid hybridisation

Braun S, Humphreys C, Fraser E, Brancale A, Bochtler M, Dale TC

PLoS One. 2011

Importance of single molecular determinants in the fidelity of expanded genetic codes

Antonczak AK, Simova Z, Yonemoto IT, Bochtler M, Piasecka A, Czapinska H, Brancale A, Tippmann EM

Proc Natl Acad Sci U S A.. 2011

DNA intercalation without flipping in the specific ThaI-DNA complex

Firczuk M, Wojciechowski M, Czapinska H, Bochtler M

Nucleic Acids Res. 2011


Crystallization of the Photosystem II core complex and its chlorophyll binding subunit CP43 from transplastomic plants of Nicotiana tabacum

Piano D, El Alaoui S, Korza HJ, Filipek R, Sabala I, Haniewicz P, Buechel C, De Sanctis D, Bochtler M

Photosynth Res. 2010

1.45 A resolution crystal structure of recombinant PNP in complex with a pM multisubstrate analogue inhibitor bearing one feature of the postulated transition state

Chojnowski G, Breer K, Narczyk M, Wielgus-Kutrowska B, Czapinska H, Hashimoto M, Hikishima S, Yokomatsu T, Bochtler M, Girstun A, Staroń K, Bzowska A

Biochem Biophys Res Commun. 2010

Alu-repeat-induced deletions within the NCF2 gene causing p67-phox-deficient chronic granulomatous disease (CGD)

Gentsch M, Kaczmarczyk A, van Leeuwen K, de Boer M, Kaus-Drobek M, Dagher MC, Kaiser P, Arkwright PD, Gahr M, Rösen-Wolff A, Bochtler M, Secord E, Britto-Williams P, Saifi GM, Maddalena A, Dbaibo G, Bustamante J, Casanova JL, Roos D, Roesler J

Hum Mutat. 2010

DIBER: protein, DNA or both?

Chojnowski G, Bochtler M

Acta Crystallogr D Biol Crystallogr. 2010


Crystal structure of the beta beta alpha-Me type II restriction endonuclease Hpy99I with target DNA

Sokolowska M, Czapinska H, Bochtler M

Nucleic Acids Res. 2009


Crystal structure and mechanism of the Staphylococcus cohnii virginiamycin B lyase (Vgb)

Lipka M, Filipek R, Bochtler M

Biochemistry. 2008

The recognition domain of the BpuJI restriction endonuclease in complex with cognate DNA at 1.3-A resolution

Sukackaite R, Grazulis S, Bochtler M, Siksnys V.

J Mol Biol. 2008

Thermodynamic studies of interactions of calf spleen PNP with acyclic phosphonate inhibitors

Breer K, Wielgus-Kutrowska B, Hashimoto M, Hikishima S, Yokomatsu T, Szczepanowski RH, Bochtler M, Girstun A, Starón K, Bzowska A

Nucleic Acids Symp Ser (Oxf). 2008

How PspGI, catalytic domain of EcoRII and Ecl18kI acquire specificities for different DNA targets

Tamulaitis G, Zaremba M, Szczepanowski RH, Bochtler M, Siksnys V

Nucleic Acids Res. 2008

Central base pair flipping and discrimination by PspGI

Szczepanowski RH, Carpenter MA, Czapinska H, Zaremba M, Tamulaitis G, Siksnys V, Bhagwat AS, Bochtler M

Nucleic Acids Res. 2008


Nucleotide flipping by restriction enzymes analyzed by 2-aminopurine steady-state fluorescence

Tamulaitis G, Zaremba M, Szczepanowski RH, Bochtler M, Siksnys V

Nucleic Acids Res. 2007

Monomeric restriction endonuclease BcnI in the apo form and in an asymmetric complex with target DNA.

Sokolowska M, Kaus-Drobek M, Czapinska H, Tamulaitis G, Szczepanowski RH, Urbanke C, Siksnys V, Bochtler M

J Mol Biol. 2007

Restriction endonucleases that resemble a component of the bacterial DNA repair machinery

Sokolowska M, Kaus-Drobek M, Czapinska H, Tamulaitis G, Siksnys V, Bochtler M

Cell Mol Life Sci. 2007

Restriction endonuclease MvaI is a monomer that recognizes its target sequence asymmetrically

Kaus-Drobek M, Czapinska H, Sokołowska M, Tamulaitis G, Szczepanowski RH, Urbanke C, Siksnys V, Bochtler M

Nucleic Acids Res. 2007

Mutational analysis of peptidoglycan amidase MepA

Firczuk M, Bochtler M

Biochemistry. 2007

Folds and activities of peptidoglycan amidases

Firczuk M, Bochtler M

FEMS Microbiol Rev. 2007

The statistics of the highest E value

Chojnowski G, Bochtler M

Acta Crystallogr A. 2007

The highest reflection intensity in a resolution shell

Bochtler M, Chojnowski G

Acta Crystallogr A. 2007


Nucleotide flips determine the specificity of the Ecl18kI restriction endonuclease

Bochtler M, Szczepanowski RH, Tamulaitis G, Grazulis S, Czapinska H, Manakova E, Siksnys V

EMBO J. 2006


Peptydoglycan amidase MepA is a LAS metallopeptidase

Marcyjaniak M, Odintsov SG, Sabala I, Bochtler M

J Biol Chem. 2005

Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases

Potempa J, Golonka E, Filipek R, Shaw LN

Mol Microbiol. 2005

Crystal structure of a fragment of mouse ubiquitin-activating enzyme.

Szczepanowski RH, Filipek R, Bochtler M

J Biol Chem. 2005

Substrate access to the active sites in aminopeptidase T, a representative of a new metallopeptidase clan.

Odintsov SG, Sabała I, Bourenkov G, Rybin V, Bochtler M

J Mol Biol. 2005

Staphylococcus aureus aminopeptidase S is a founding member of a new peptidase clan

Odintsov SG, Sabała I, Bourenkov G, Rybin V, Bochtler M

J Biol Chem. 2005

Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow.

Korza HJ, Bochtler M

J Biol Chem. 2005

Molecular machines for protein degradation.

Groll M, Bochtler M, Brandstetter H, Clausen T, Huber R

Chembiochem. 2005

Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease.

Grazulis S, Manakova E, Roessle M, Bochtler M, Tamulaitiene G, Huber R, Siksnys V

Proc Natl Acad Sci U S A. 2005

Crystal structures of active LytM

Firczuk M, Mucha A, Bochtler M

J Mol Biol. 2005

A comparison of staphostatin B with standard mechanism serine protease inhibitors

Filipek R, Potempa J, Bochtler M

J Biol Chem. 2005

Escherichia coli purine nucleoside phosphorylase II, the product of the xapA gene

Dandanell G,Szczepanowski RH, Kierdaszuk B, Shugar D, Bochtler M

J Mol Biol. 2005

Characterization of the HslU chaperone affinity for HslV protease

Azim MK, Goehring W, Song HK, Ramachandran R, Bochtler M, Goettig P

Protein Sci. 2005


Genetic characterization of staphopain genes in Staphylococcus aureus

Golonka E, Filipek R, Sabat A, Sinczak A, Potempa J

Biol Chem. 2004

Latent LytM at 1.3A resolution

Odintsov SG, Sabala I, Marcyjaniak M, Bochtler M

J Mol Biol. 2004

Peptidoglycan amidase MepA is a LAS metallopeptidase

Marcyjaniak M, Odintsov SG, Sabala I, Bochtler M

J Biol Chem. 2004

Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition

Filipek R, Szczepanowski R, Sabat A, Potempa J, Bochtler M

Biochemistry. 2004

Similar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases.

Bochtler M, Odintsov SG, Marcyjaniak M, Sabala I

Protein Sci. 2004

Peptidoglycan amidase MepA is a LAS metallopeptidase.

Marcyjaniak M, Odintsov SG, Sabala I, Bochtler M

J Biol Chem. 2004


Staphostatins resemble lipocalins, not cystatins in fold

Rzychon M, Filipek R, Sabat A, Kosowska K, Dubin A, Potempa J, Bochtler M

Protein Sci. 2003

The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease.

Filipek R, Rzychon M, Oleksy A, Gruca M, Dubin A, Potempa J, Bochtler M

J Biol Chem. 2003

A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus.

Dubin G, Krajewski M, Popowicz G, Stec-Niemczyk J, Bochtler M, Potempa J, Dubin A, Holak TA

Biochemistry. 2003


Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY)

Ramachandran R, Hartmann C, Song HK, Huber R, Bochtler M

Proc Natl Acad Sci U S A. 2002


Structural and biochemical characterization of neuronal calretinin domain I-II (residues 1-100). Comparison to homologous calbindin D28k domain I-II (residues 1-93)

Palczewska M, Groves P, Ambrus A, Kaleta A, Kövér KE, Batta G, Kuźnicki J.

Eur J Biochem.. 2001