Scholars@Duke
Harold Paul Erickson

Harold Paul Erickson

James B. Duke Distinguished Professor Emeritus of Cell Biology
Cell Biology
Duke Box 3709, Durham, NC 27710
x, Durham, NC 27710

Featured Works

Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.

Journal article J Biol Chem · July 29, 2011 Featured Publication Fibronectin (FN) is an extracellular matrix protein that is assembled into fibrils by cells during tissue morphogenesis and wound healing. FN matrix fibrils are highly elastic, but the mechanism of elasticity has been debated: it may be achieved by mechani ... Full text Open Access Link to item Cite

Inside-out Z rings--constriction with and without GTP hydrolysis.

Journal article Mol Microbiol · July 2011 Featured Publication The bacterial tubulin homologue FtsZ forms a ring-like structure called the Z ring that drives cytokinesis. We showed previously that FtsZ-YFP-mts, which has a short amphipathic helix (mts) on its C terminus that inserts into the membrane, can assemble con ... Full text Open Access Link to item Cite

Conformational changes of FtsZ reported by tryptophan mutants.

Journal article Biochemistry · May 31, 2011 Featured Publication E. coli FtsZ has no native tryptophan. We showed previously that the mutant FtsZ L68W gave a 2.5-fold increase in trp fluorescence when assembly was induced by GTP. L68 is probably buried in the protofilament interface upon assembly, causing the fluorescen ... Full text Open Access Link to item Cite

FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.

Journal article Microbiol Mol Biol Rev · December 2010 Featured Publication FtsZ, a bacterial homolog of tubulin, is well established as forming the cytoskeletal framework for the cytokinetic ring. Recent work has shown that purified FtsZ, in the absence of any other division proteins, can assemble Z rings when incorporated inside ... Full text Open Access Link to item Cite

Cell division without FtsZ--a variety of redundant mechanisms.

Journal article Mol Microbiol · October 2010 Featured Publication Full text Open Access Link to item Cite

Suprastructures and dynamic properties of Mycobacterium tuberculosis FtsZ.

Journal article J Biol Chem · April 9, 2010 Featured Publication Tuberculosis causes the most death in humans by any bacterium. Drug targeting of bacterial cytoskeletal proteins requires detailed knowledge of the various filamentous suprastructures and dynamic properties. Here, we have investigated by high resolution el ... Full text Link to item Cite

Curved FtsZ protofilaments generate bending forces on liposome membranes.

Journal article EMBO J · November 18, 2009 Featured Publication We have created FtsZ-YFP-mts where an amphipathic helix on the C-terminus tethers FtsZ to the membrane. When incorporated inside multi-lamellar tubular liposomes, FtsZ-YFP-mts can assemble Z rings that generate a constriction force. When added to the outsi ... Full text Open Access Link to item Cite

Structural determinants of autoproteolysis of the Haemophilus influenzae Hap autotransporter.

Journal article Infect Immun · November 2009 Featured Publication Haemophilus influenzae is a gram-negative bacterium that initiates infection by colonizing the upper respiratory tract. The H. influenzae Hap autotransporter protein mediates adherence, invasion, and microcolony formation in assays with respiratory epithel ... Full text Link to item Cite

BtubA-BtubB heterodimer is an essential intermediate in protofilament assembly.

Journal article PLoS One · September 29, 2009 Featured Publication BACKGROUND: BtubA and BtubB are two tubulin-like genes found in the bacterium Prosthecobacter. Our work and a previous crystal structure suggest that BtubB corresponds to alpha-tubulin and BtubA to beta-tubulin. A 1:1 mixture of the two proteins assembles ... Full text Link to item Cite

FtsZ filament dynamics at steady state: subunit exchange with and without nucleotide hydrolysis.

Journal article Biochemistry · July 21, 2009 Featured Publication We have measured three aspects of FtsZ filament dynamics at steady state: rates of GTP hydrolysis, subunit exchange between protofilaments, and disassembly induced by dilution or excess GDP. All three reactions were slowed with an increase in the potassium ... Full text Link to item Cite

Modeling the physics of FtsZ assembly and force generation.

Journal article Proc Natl Acad Sci U S A · June 9, 2009 Featured Publication The tubulin homolog FtsZ is the major cytoskeletal protein in bacterial cytokinesis. It can generate a constriction force on the bacterial membrane or inside tubular liposomes. Several models have recently been proposed for how this force might be generate ... Full text Link to item Cite

Transient opening of fibronectin type III (FNIII) domains: the interaction of the third FNIII domain of FN with anastellin.

Journal article Biochemistry · May 19, 2009 Featured Publication We previously reported that the fibronectin (FN) type III domains of FN may unfold to interact with anastellin and form FN aggregates. In the present study, we have focused on the interaction between anastellin and the third FN type III domain (III3), whic ... Full text Link to item Cite

Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy.

Journal article Biol Proced Online · May 15, 2009 Featured Publication An important part of characterizing any protein molecule is to determine its size and shape. Sedimentation and gel filtration are hydrodynamic techniques that can be used for this medium resolution structural analysis. This review collects a number of simp ... Full text Link to item Cite

FtsZ condensates: an in vitro electron microscopy study.

Journal article Biopolymers · May 2009 Featured Publication In vivo cell division protein FtsZ from E. coli forms rings and spirals which have only been observed by low resolution light microscopy. We show that these suprastructures are likely formed by molecular crowding which is a predominant factor in prokaryoti ... Full text Link to item Cite

Revisiting the mystery of fibronectin multimers: the fibronectin matrix is composed of fibronectin dimers cross-linked by non-covalent bonds.

Journal article Matrix Biol · April 2009 Featured Publication Fibronectin (FN) matrix fibrils have long been thought to be formed by disulfide-bonded FN multimers, although there is no direct evidence that they are covalently linked with each other. To understand the biochemical properties of these fibrils, we extrac ... Full text Link to item Cite

Display of cell surface sites for fibronectin assembly is modulated by cell adherence to (1)F3 and C-terminal modules of fibronectin.

Journal article PLoS One · 2009 Featured Publication BACKGROUND: Fibronectin-null cells assemble soluble fibronectin shortly after adherence to a substrate coated with intact fibronectin but not when adherent to the cell-binding domain of fibronectin (modules (7)F3-(10)F3). Interactions of adherent cells wit ... Full text Open Access Link to item Cite

Chapter 1 - Tubular liposomes with variable permeability for reconstitution of FtsZ rings.

Journal article Methods Enzymol · 2009 Featured Publication We have developed a system for producing tubular multilamellar liposomes that incorporate the protein FtsZ on the inside. We start with a mixture of spherical multilamellar liposomes with FtsZ initially on the outside. Shearing forces generated by applying ... Full text Open Access Link to item Cite

The coiled coils of cohesin are conserved in animals, but not in yeast.

Journal article PLoS One · 2009 Featured Publication BACKGROUND: The SMC proteins are involved in DNA repair, chromosome condensation, and sister chromatid cohesion throughout Eukaryota. Long, anti-parallel coiled coils are a prominent feature of SMC proteins, and are thought to serve as spacer rods to provi ... Full text Link to item Cite

The RGD motif in fibronectin is essential for development but dispensable for fibril assembly.

Journal article J Cell Biol · July 2, 2007 Featured Publication Fibronectin (FN) is secreted as a disulfide-bonded FN dimer. Each subunit contains three types of repeating modules: FN-I, FN-II, and FN-III. The interactions of alpha5beta1 or alphav integrins with the RGD motif of FN-III repeat 10 (FN-III10) are consider ... Full text Link to item Cite

Evolution of the cytoskeleton.

Journal article Bioessays · July 2007 Featured Publication The eukaryotic cytoskeleton appears to have evolved from ancestral precursors related to prokaryotic FtsZ and MreB. FtsZ and MreB show 40-50% sequence identity across different bacterial and archaeal species. Here I suggest that this represents the limit o ... Full text Link to item Cite

An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins.

Journal article Protein Sci · July 2007 Featured Publication We have experimentally studied the fluorescence resonance energy transfer (FRET) between green fluorescent protein (GFP) molecules by inserting folded or intrinsically unstructured proteins between CyPet and Ypet. We discovered that most of the enhanced FR ... Full text Link to item Cite

FtsZ from divergent foreign bacteria can function for cell division in Escherichia coli.

Journal article J Bacteriol · October 2006 Featured Publication FtsZs from Mycoplasma pulmonis (MpuFtsZ) and Bacillus subtilis (BsFtsZ) are only 46% and 53% identical in amino acid sequence to FtsZ from Escherichia coli (EcFtsZ). In the present study we show that MpuFtsZ and BsFtsZ can function for cell division in E. ... Full text Link to item Cite

Sequence divergence of coiled coils--structural rods, myosin filament packing, and the extraordinary conservation of cohesins.

Journal article J Struct Biol · May 2006 Featured Publication The amino acid sequences of the long, anti-parallel coiled coils of the cohesin subunits SMC1 and SMC3 are almost totally conserved in mammals. To understand this exceptional conservation more broadly, we analyzed amino acid sequence variation for several ... Full text Link to item Cite

Probing the domain structure of FtsZ by random truncation and insertion of GFP.

Journal article Microbiology (Reading) · December 2005 Featured Publication Random transposon-mediated mutagenesis has been used to create truncations and insertions of green fluorescent protein (GFP), and Venus-yellow fluorescent protein (YFP), in Escherichia coli FtsZ. Sixteen unique insertions were obtained, and one of them, in ... Full text Link to item Cite

Domain unfolding plays a role in superfibronectin formation.

Journal article J Biol Chem · November 25, 2005 Featured Publication Superfibronectin (sFN) is a fibronectin (FN) aggregate that is formed by mixing FN with anastellin, a fragment of the first type III domain of FN. However, the mechanism of this aggregation has not been clear. In this study, we found that anastellin co-pre ... Full text Link to item Cite

Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer.

Journal article J Biol Chem · June 10, 2005 Featured Publication We have developed an assay for the assembly of FtsZ based on fluorescence resonance energy transfer (FRET). We mutated an innocuous surface residue to cysteine and labeled separate pools with fluorescein (donor) and tetramethylrhodamine (acceptor). When th ... Full text Link to item Cite

In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB.

Journal article J Cell Biol · April 25, 2005 Featured Publication Arecent study identified genuine tubulin proteins, BtubA and BtubB, in the bacterial genus Prosthecobacter. We have expressed BtubA and BtubB in Escherichia coli and studied their in vitro assembly. BtubB by itself formed rings with an outer diameter of 35 ... Full text Link to item Cite

Mutants of FtsZ targeting the protofilament interface: effects on cell division and GTPase activity.

Journal article J Bacteriol · April 2005 Featured Publication The bacterial cell division protein FtsZ assembles into straight protofilaments, one subunit thick, in which subunits appear to be connected by identical bonds or interfaces. These bonds involve the top surface of one subunit making extensive contact with ... Full text Link to item Cite

A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus.

Journal article Biophys J · January 2005 Featured Publication FtsZ is the major cytoskeletal protein operating in bacterial cell division. FtsZ assembles into protofilaments in vitro, and there has been some controversy over whether the assembly is isodesmic or cooperative. Assembly has been assayed previously by sed ... Full text Link to item Cite

Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.

Journal article J Bacteriol · September 2004 Featured Publication FtsZ is the major cytoskeletal component of the bacterial cell division machinery. It forms a ring-shaped structure (the Z ring) that constricts as the bacterium divides. Previous in vivo experiments with green fluorescent protein-labeled FtsZ and fluoresc ... Full text Link to item Cite

The disulfide bonding pattern in ficolin multimers.

Journal article J Biol Chem · February 20, 2004 Featured Publication Ficolin is a plasma lectin, consisting of a short N-terminal multimerization domain, a middle collagen domain, and a C-terminal fibrinogen-like domain. The collagen domains assemble the subunits into trimers, and the N-terminal domain assembles four trimer ... Full text Link to item Cite

In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function.

Journal article J Bacteriol · August 2003 Featured Publication We have characterized the in vivo phenotypes of 17 mutations of Escherichia coli ftsZ. In particular, we determined whether these mutations can complement a null ftsZ phenotype, and we demonstrated that two noncomplementing mutations show partial dominant- ... Full text Link to item Cite

Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants.

Journal article J Cell Sci · March 15, 2002 Featured Publication We have prepared 3T3 cells doubly labeled to visualize simultaneously the extracellular fibronectin (FN) matrix and intracellular actin cytoskeleton in living cell cultures. We used FN-yellow fluorescent protein (FN-yfp) for the FN matrix, and the actin-bi ... Full text Link to item Cite

Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching.

Journal article Proc Natl Acad Sci U S A · March 5, 2002 Featured Publication FtsZ, the major cytoskeletal component of the bacterial cell-division machine, assembles into a ring (the Z-ring) that contracts at septation. FtsZ is a bacterial homolog of tubulin, with similar tertiary structure, GTP hydrolysis, and in vitro assembly. W ... Full text Link to item Cite

Stretching fibronectin.

Journal article J Muscle Res Cell Motil · 2002 Featured Publication Fibronectin (FN) matrix fibrils assembled in cell culture have been observed to stretch in response to cell movements, and when broken relax to 1/3 to 1/4 of their rest length. Two molecular mechanisms have been proposed, for the elasticity. One proposes t ... Full text Link to item Cite

Gamma-tubulin nucleation: template or protofilament?

Journal article Nat Cell Biol · June 2000 Featured Publication Gamma-tubulin is known to nucleate microtubule assembly from alpha/beta-tubulin, but the molecular mechanism by which this process occurs is the subject of some controversy. Four recent papers have provided new structural and biochemical constraints on the ... Full text Link to item Cite

Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis.

Journal article J Cell Biol · April 17, 2000 Featured Publication Fibronectin's RGD-mediated binding to the alpha5beta1 integrin is dramatically enhanced by a synergy site within fibronectin III domain 9 (FN9). Guided by the crystal structure of the cell-binding domain, we selected amino acids in FN9 that project in the ... Full text Link to item Cite

Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein.

Journal article Proc Natl Acad Sci U S A · March 2, 1999 Featured Publication Fibronectin (FN) forms the primitive fibrillar matrix in both embryos and healing wounds. To study the matrix in living cell cultures, we have constructed a cell line that secretes FN molecules chimeric with green fluorescent protein. These FN-green fluore ... Full text Link to item Cite

Oligomeric structure and tissue distribution of ficolins from mouse, pig and human.

Journal article Arch Biochem Biophys · December 15, 1998 Featured Publication Mouse plasma ficolin was purified by GlcNAc affinity and anion-exchange chromatography. Gel-filtration chromatography and gradient sedimentation indicated that mouse plasma ficolin is a 12-mer of approximately 35 kDa subunits, and electron microscopy showe ... Full text Link to item Cite

The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge.

Journal article J Cell Biol · September 21, 1998 Featured Publication Structural maintenance of chromosomes (SMC) proteins function in chromosome condensation and several other aspects of DNA processing. They are large proteins characterized by an NH2-terminal nucleotide triphosphate (NTP)-binding domain, two long segments o ... Full text Link to item Cite

How calcium causes microtubule depolymerization.

Journal article Cell Motil Cytoskeleton · 1997 Featured Publication The effects of calcium (Ca) were assessed using video-enhanced differential interference contrast light microscopy on individual microtubules in vitro. Phosphocellulose-purified (PC) and microtubule associated protein (MAP)-containing preparations of porci ... Full text Link to item Cite

2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region.

Journal article Cell · January 12, 1996 Featured Publication We have determined the 2.0 A crystal structure of a fragment of human fibronectin encompassing the seventh through the RGD-containing tenth type III repeats (FN7-10). The structure reveals an extended rod-like molecule with a long axis of approximately 140 ... Full text Link to item Cite

Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers.

Journal article Proc Natl Acad Sci U S A · January 9, 1996 Featured Publication The bacterial cell division protein FtsZ is a homolog of tubulin, but it has not been determined whether FtsZ polymers are structurally related to the microtubule lattice. In the present study, we have obtained high-resolution electron micrographs of two F ... Full text Link to item Cite

Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin.

Journal article Proc Natl Acad Sci U S A · October 11, 1994 Featured Publication The elastic protein titin comprises a tandem array of fibronectin type III and immunoglobulin domains, which are structurally similar 7-strand beta-sandwiches. A proposed mechanism for stretching titin, by sequential denaturation of individual fibronectin ... Full text Link to item Cite

Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein.

Journal article Science · November 6, 1992 Featured Publication Fibronectin type III domains are found in many different proteins including cell surface receptors and cell adhesion molecules. The crystal structure of one such domain from the extracellular matrix protein tenascin was determined. The structure was solved ... Full text Link to item Cite

Kinetics of protein-protein association explained by Brownian dynamics computer simulation.

Journal article Proc Natl Acad Sci U S A · April 15, 1992 Featured Publication Protein-protein bond formations, such as antibody-antigen complexation or aggregation of protein monomers into dimers and larger aggregates, occur with bimolecular rate constants on the order of 10(6) M-1.s-1, which is only 3 orders of magnitude slower tha ... Full text Link to item Cite

Co-operativity in protein-protein association. The structure and stability of the actin filament.

Journal article J Mol Biol · April 5, 1989 Featured Publication Co-operative association, in which a protein subunit is held simultaneously by two bonds, is enormously more favorable than association forming either bond alone. A theoretical framework for calculating the effect of co-operativity is developed here, which ... Full text Link to item Cite

Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies.

Journal article J Cell Biol · October 1988 Featured Publication We have developed video microscopy methods to visualize the assembly and disassembly of individual microtubules at 33-ms intervals. Porcine brain tubulin, free of microtubule-associated proteins, was assembled onto axoneme fragments at 37 degrees C, and th ... Full text Link to item Cite

A six-armed oligomer isolated from cell surface fibronectin preparations.

Journal article Nature · September 20, 1984 Featured Publication Fibronectins are adhesive glycoproteins thought to mediate the attachment of cells to various substrates. Plasma fibronectin (PFN) is a dimer comprising subunits of molecular weight 220,000, connected by one or two disulphide bonds. Electron microscopy sho ... Full text Link to item Cite

The kinetics of microtubule assembly. Evidence for a two-stage nucleation mechanism.

Journal article J Biol Chem · August 25, 1984 Featured Publication A model describing the nucleation and assembly of purified tubulin has been developed. The novel feature of this model is a two stage nucleation process to allow the explicit inclusion of the two-dimensional nature of the early stages of microtubule assemb ... Link to item Cite

Microtubule surface lattice and subunit structure and observations on reassembly.

Journal article J Cell Biol · January 1974 Featured Publication Neuronal microtubules have been reassembled from brain tissue homogenates and purified. In reassembly from purified preparations, one of the first structures formed was a flat sheet, consisting of up to 13 longitudinal filaments, which was identified as an ... Full text Link to item Cite