Gender	Female
E-mail	terry.krulwich@mssm.edu
Education and Training	B.A., Goucher College
	M.S., Ph.D., University of Wisconsin
	NSF Pre-Doctoral Fellowship, Albert Einstein College of Medicine
	NSF Post-Doctoral Fellowship, Albert Einstein College of Medicine

Dr. Krulwich is the Sharon & Frederick A. Klingenstein-Nathan G. Kase, MD Professor, Program Director of the Mount Sinai Post-Baccalaureate Research Education Program and of the pre-doctoral Integrated Pharmacological Sciences Training Program.  She is also Education and Outreach Core Director for the Systems Biology Center New York.  Dr. Krulwich's research programs are described under the Krulwich Laboratory.

Education and Training	B.A., Goucher College
	M.S., Ph.D., University of Wisconsin
	NSF Pre-Doctoral Fellowship, Albert Einstein College of Medicine
	NSF Post-Doctoral Fellowship, Albert Einstein College of Medicine

Summary of Research

We study ion-translocating membrane transporters in bacterial cells are critical participants in the physiology of both pathogens and non-pathogenic bacteria of ecological interest.

1. Mrp-type monovalent cation/proton antiporter systems: basis and roles for the unusual complexity of this major bacterial antiporter system. In collaboration with Masahiro Ito's lab (Toyo University, Japan), we study the catalytic properties, physiological roles and structural features of Mrp systems from bacteria such as pathogenic Staphylococcus aureus and non-pathogenic Bacillus species. We are testing the hypothesis that Mrp proteins form a complex that is a "consortium" of transporters, including monovalent cation/proton antiporters, that function synergistically. A systems analysis combined with genetic and biochemical experiments are testing a hypothesis to explain how the Mrp-like transporter Mnh1 of S. aureus leads to a higher membrane potential and susceptibility to antimicrobial peptides than is found in mutants with disrupted Mnh1, the opposite effect expected from a membrane potential-consuming antiporter.

2. Oxidative phosphorylation at high pH: a model system for probing the proton path during energization of ATP synthesis by the respiratory chain. Biochemical, molecular and biophysical studies of OXPHOS in membranes and purified systems test the hypothesis of sequestered proton transfer during OXPHOS. This work has revealed special adaptations of the ATP synthase are required for function at high pH.

3. Novel catalytic roles in ammonium transport have recently been supported for a group of bacterial transporters and a role in pH regulation via anion exchanges are suggested by recent work for a transporter group that is widely distributed among bacteria. The physiological roles that these transporters are playing will be clarified and may lead to new opportunities for growth inhibition.

Dr. Krulwich also leads an NIH-supported educational study on factors that enhance the successful post-baccalaureate intervention to promote research careers (ESPI study). The hypotheses to be tested in the ESPI study emerged from observations made during the initial period of Dr. Krulwich's directorship of Mount Sinai's Post-baccalaureate Research Education Program.

Liu J, Fujisawa M, Hicks DB, Krulwich TA. Characterization of the functionally critical AXAXAXA and PXXEXXP motifs of the ATP synthase c-subunit from an alkaliphilic Bacillus. J Biol Chem 2009 March; 284(13): 8714-8725.

Dzioba-Winogrodzki J, Winogrodzki O, Krulwich TA, Boin MA, Hase CC, Dibrov P. The Vibrio cholerae Mrp system: cation/proton antiport properties and enhancement of bile salt resistance in a heterologous host. J Mol Microbiol Biotechnol 2009 March; 16(3-4): 176-186.

Terahara N, Krulwich TA, Ito M. Mutations alter the sodium versus proton use of a Bacillus clausii flagellar motor and confer dual ion use on Bacillus subtilis motors. Proc Natl Acadm Sci U S A 2008 Sept 23; 105(38): 14359-143564.

Morino M, Natsui S, Swartz TH, Krulwich TA, Ito M. Single gene deletions of mrpA to mrpG and mrpE point mutations affect activity of the Mrp Na+/H+ antiporter of alkaliphilic Bacillus and formation of hetero-oligomeric Mrp complexes. J Bacteriol 2008 Jun; 190(12): 4162-4172.

Liu J, Krulwich TA, Hicks DB. Purification of two putative type II NADH dehydrogenases with different substrate specificities from alkaliphilic Bacillus pseudofirmus OF4. Biochim Biophys Acta 2008 May; 1777(5): 453-461.

Fujinami S, Sato T, Trimmer JS, Spiller BW, Clapham DE, Krulwich TA, Kawagishi I, Ito M. The voltage-gated Na+ channel NaVBP co-localizes with methyl-accepting chemotaxis protein at cell poles of alkaliphilic Bacillus pseudofirmus OF4. Microbiology 2007 Dec; 153(Pt 12): 4027-38.

Fujisawa M, Ito M, Krulwich TA. Three two-component transporters with channel-like properties have monovalent cation/proton antiport activity. Proc Natl Acad Sci U S A 2007 Aug 14; 104(33): 13289-94.

Wei Y, Liu J, Ma Y, Krulwich TA. Three putative cation/proton antiporters from the soda lake alkaliphile Alkalimonas amylolytica N10 complement an alkali-sensitive Escherichia coli mutant. Microbiology 2007 July; 153(Pt 7): 2168-2179.

Swartz TH, Ito M, Ohira T, Natsui S, Hicks DB, Krulwich TA. Catalytic properties of Staphylococcus aureus and Bacillus members of the secondary cation/proton antiporter-3 (Mrp) family are revealed by an optimized assay in an Escherichia coli host. J Bacteriol 2007 April; 189(8): 3081-3090.

Liu X, Gong X, Hicks DB, Krulwich TA, Yu L, Yu CA. Interaction between cytochrome caa3 and F1F0-ATP synthase of alkaliphilic Bacillus pseudofirmus OF4 is demonstrated by saturation transfer electron paramagnetic resonance and differential scanning calorimetry assays. Biochemistry 2007 Jan 9; 46(1): 306-313.