Sevier, Carolyn S., Kadokura, Hiroshi, Tam, Vincent C., Beckwith, Jon, Fass, Deborah, Kaiser, Chris A.
Three different classes of thiol-oxidoreductases that facilitate the formation of protein disulfide bonds have been identified. They are the Ero1 and SOX/ALR family members in eukaryotic cells, and...
Goehring, Nathan W., Gueiros-Filho, Frederico, Beckwith, Jon
Cell division in Escherichia coli requires the recruitment of at least 10 essential proteins to the bacterial midcell. Recruitment of these proteins follows a largely linear dependency pathway in...
Jennifer A. Leeds, Dana Boyd, Damon R. Huber, G. Koji Sonoda, Hieu T. Luu, Donald M. Engelman, ...
Introduction Integral membrane proteins play essential roles in numerous cellular functions, including cell division, intra and inter-cellular signaling, and transport of macromolecules. 14 Mutations...
Precis of Vaulting Ambition: Sociobiology and the Quest for Human Nature (1987)
Kitcher, Philip, Bateson, Patrick, Beckwith, Jon, Bernstein, Irwin S., Smith Churchland, Patricia, Draper, Patricia, ...
The debate about the credentials of sociobiology has persisted because scholars have failed to distinguish the varieties of sociobiology and because too little attention has been paid to the details...
Tian, Hongping, Boyd, Dana, Beckwith, Jon
We describe an Escherichia coli genetic screen that yields mutations affecting two different cellular processes: disulfide bond formation and membrane protein assembly. The mutants defective in...
Pogliano, Joe, Pogliano, Kit, Weiss, David S., Losick, Richard, Beckwith, Jon
A universally conserved event in cell division is the formation of a cytokinetic ring at the future site of division. In the bacterium Escherichia coli, this ring is formed by the essential cell...
Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
Bessette, Paul H., Åslund, Fredrik, Beckwith, Jon, Georgiou, George
Under physiological conditions, the Escherichia coli cytoplasm is maintained in a reduced state that strongly disfavors the formation of stable disulfide bonds in proteins. However, mutants in which...
Åslund, Fredrik, Zheng, Ming, Beckwith, Jon, Storz, Gisela
The Escherichia coli transcription factor OxyR is activated by the formation of an intramolecular disulfide bond and subsequently is deactivated by enzymatic reduction of the disulfide bond. Here we...
Kadokura, Hiroshi, Bader, Martin, Tian, Hongping, Bardwell, James C. A., Beckwith, Jon
The active-site cysteines of DsbA, the periplasmic disulfide-bond-forming enzyme of Escherichia coli, are kept oxidized by the cytoplasmic membrane protein DsbB. DsbB, in turn, is oxidized by two...
Debarbieux, Laurent, Beckwith, Jon
Thioredoxin 1 is a major thiol-disulfide oxidoreductase in the cytoplasm of Escherichia coli. One of its functions is presumed to be the reduction of the disulfide bond in the active site of the...
DsbC activation by the N-terminal domain of DsbD
Goldstone, David, Haebel, Peter W., Katzen, Federico, Bader, Martin W., Bardwell, James C. A., Beckwith, Jon, ...
The correct formation of disulfide bonds in the periplasm of Escherichia coli involves Dsb proteins, including two related periplasmic disulfide-bond isomerases, DsbC and DsbG. DsbD is a membrane...
Weiss, David S., Chen, Joseph C., Ghigo, Jean-Marc, Boyd, Dana, Beckwith, Jon
Assembly of the division septum in bacteria is mediated by several proteins that localize to the division site. One of these, FtsI (also called penicillin-binding protein 3) of Escherichia coli,...
Septal Localization of FtsQ, an Essential Cell Division Protein in Escherichia coli
Chen, Joseph C., Weiss, David S., Ghigo, Jean-Marc, Beckwith, Jon
Septation in Escherichia coli requires several gene products. One of these, FtsQ, is a simple bitopic membrane protein with a short cytoplasmic N terminus, a membrane-spanning segment, and a...
Ghigo, Jean-Marc, Beckwith, Jon
In Escherichia coli, nine essential cell division proteins are known to localize to the division septum. FtsL is a 13-kDa bitopic membrane protein with a short cytoplasmic N-terminal domain, a...
Debarbieux, Laurent, Beckwith, Jon
Escherichia coli thioredoxin 1 has been characterized in vivo and in vitro as one of the most efficient reductants of disulfide bonds. Nevertheless, under some conditions, thioredoxin 1 can also act...
Boyd, Dana, Weiss, David S., Chen, Joseph C., Beckwith, Jon
We describe a simple system for reversible, stable integration of plasmid-borne genes into the Escherichia coli chromosome. Most ordinary E. coli strains and a variety of pBR322-derived...
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA
Kadokura, Hiroshi, Beckwith, Jon
Protein disulfide bond formation in Escherichia coli is catalyzed by the periplasmic protein DsbA. A cytoplasmic membrane protein DsbB maintains DsbA in the oxidized state by transferring electrons...
Katzen, Federico, Deshmukh, Meenal, Daldal, Fevzi, Beckwith, Jon
Modular organization of proteins has been postulated as a widely used strategy for protein evolution. The multidomain transmembrane protein DsbD catalyzes the transfer of electrons from the cytoplasm...
Haebel, Peter W., Goldstone, David, Katzen, Federico, Beckwith, Jon, Metcalf, Peter
The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDα) of...
We describe the further utilization of a genetic screen that identifies mutations defective in the assembly of proteins into the Escherichia coli cytoplasmic membrane. The screen yielded mutations in...
Chen, Joseph C., Minev, Michael, Beckwith, Jon
FtsQ, a 276-amino-acid, bitopic membrane protein, is one of the nine proteins known to be essential for cell division in gram-negative bacterium Escherichia coli. To define residues in FtsQ critical...
Katzen, Federico, Beckwith, Jon
The central hydrophobic domain of the membrane protein DsbD catalyzes the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. Two cysteine residues embedded in...
Schierle, Clark F., Berkmen, Mehmet, Huber, Damon, Kumamoto, Carol, Boyd, Dana, Beckwith, Jon
The Escherichia coli cytoplasmic protein thioredoxin 1 can be efficiently exported to the periplasmic space by the signal sequence of the DsbA protein (DsbAss) but not by the signal sequence of...
FtsL, an Essential Cytoplasmic Membrane Protein Involved in Cell Division in Escherichia coli
Guzman, Luz-Maria, Barondess, James J., Beckwith, Jon
We have identified a gene involved in bacterial cell division, located immediately upstream of the ftsI gene in the min 2 region of the Escherichia coli chromosome. This gene, which we named ftsL,...
Deletion of the Escherichia coli crp Gene
Sabourin, Dennis, Beckwith, Jon
Spontaneous crp mutants Escherichia coli were selected from a strain that does not require 3′,5′-cyclic adenosine monophosphate for CAP activity. Several deletions of the crp gene were...
Cyclic Adenosine Monophosphate-Independent Mutants of the Lactose Operon of Escherichia coli
Arditti, Rita, Grodzicker, Terri, Beckwith, Jon
In Escherichia coli the transcription of the lactose operon, like other catabolite-sensitive operons, requires catabolite gene activator protein and 3′,5′-cyclic adenosine monophosphate in...
Brickman, Edith, Soll, Larry, Beckwith, Jon
Sixty-two spontaneous mutations have been characterized which reduce the level of expression of catabolite-sensitive operons. These mutations appear to affect either the crp (catabolite gene...
Mechanism of Activation of Catabolite-Sensitive Genes: A Positive Control System*
Zubay, Geoffrey, Schwartz, Daniele, Beckwith, Jon
Catabolite repression is defined as the inhibition of enzyme induction by glucose or related substances. In the bacterium E. coli, the effect of glucose appears to be due to a lowering of the cyclic...
Ortenberg, Ron, Gon, Stéphanie, Porat, Amir, Beckwith, Jon
A strain of Escherichia coli missing three members of the thioredoxin superfamily, thioredoxins 1 and 2 and glutaredoxin 1, is unable to grow, a phenotype presumed to be due to the inability of cells...
Goehring, Nathan W., Gueiros-Filho, Frederico, Beckwith, Jon
Cell division in Escherichia coli requires the recruitment of at least 10 essential proteins to the bacterial midcell. Recruitment of these proteins follows a largely linear dependency pathway in...
Kadokura, Hiroshi, Nichols, Lorenzo, Beckwith, Jon
The DsbA-DsbB pathway introduces disulfide bonds into newly translocated proteins. Conversion of the conserved cis proline 151 of DsbA to several hydrophilic residues results in accumulation of mixed...
Huber, Damon, Boyd, Dana, Xia, Yu, Olma, Michael H., Gerstein, Mark, Beckwith, Jon
We have previously reported that the DsbA signal sequence promotes efficient, cotranslational translocation of the cytoplasmic protein thioredoxin-1 via the bacterial signal recognition particle...
A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo
Huber, Damon, Cha, Myoung-il, Debarbieux, Laurent, Planson, Anne-Gaëlle, Cruz, Nelly, López, Gary, ...
Escherichia coli thioredoxin is normally a cytoplasmic protein involved in the reduction of disulfide bonds. However, thioredoxin can be translocated to the periplasm when it is attached to a...
Cho, Seung-Hyun, Beckwith, Jon
The cytoplasmic membrane protein DsbD keeps the periplasmic disulfide isomerase DsbC reduced, using the cytoplasmic reducing power of thioredoxin. DsbD contains three domains, each containing two...
Reply to Hook and Lowden: the definition and implications of genetic discrimination.
Billings, Paul R, Alper, Joseph S, Beckwith, Jon, Barash, Carol I, Natowicz, Marvin R
Tian, Hongping, Boyd, Dana, Beckwith, Jon
We describe an Escherichia coli genetic screen that yields mutations affecting two different cellular processes: disulfide bond formation and membrane protein assembly. The mutants defective in...
Pogliano, Joe, Pogliano, Kit, Weiss, David S., Losick, Richard, Beckwith, Jon
A universally conserved event in cell division is the formation of a cytokinetic ring at the future site of division. In the bacterium Escherichia coli, this ring is formed by the essential cell...
Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
Bessette, Paul H., Åslund, Fredrik, Beckwith, Jon, Georgiou, George
Under physiological conditions, the Escherichia coli cytoplasm is maintained in a reduced state that strongly disfavors the formation of stable disulfide bonds in proteins. However, mutants in which...
Åslund, Fredrik, Zheng, Ming, Beckwith, Jon, Storz, Gisela
The Escherichia coli transcription factor OxyR is activated by the formation of an intramolecular disulfide bond and subsequently is deactivated by enzymatic reduction of the disulfide bond. Here we...
Kadokura, Hiroshi, Bader, Martin, Tian, Hongping, Bardwell, James C. A., Beckwith, Jon
The active-site cysteines of DsbA, the periplasmic disulfide-bond-forming enzyme of Escherichia coli, are kept oxidized by the cytoplasmic membrane protein DsbB. DsbB, in turn, is oxidized by two...
Debarbieux, Laurent, Beckwith, Jon
Thioredoxin 1 is a major thiol-disulfide oxidoreductase in the cytoplasm of Escherichia coli. One of its functions is presumed to be the reduction of the disulfide bond in the active site of the...
DsbC activation by the N-terminal domain of DsbD
Goldstone, David, Haebel, Peter W., Katzen, Federico, Bader, Martin W., Bardwell, James C. A., Beckwith, Jon, ...
The correct formation of disulfide bonds in the periplasm of Escherichia coli involves Dsb proteins, including two related periplasmic disulfide-bond isomerases, DsbC and DsbG. DsbD is a membrane...
Weiss, David S., Chen, Joseph C., Ghigo, Jean-Marc, Boyd, Dana, Beckwith, Jon
Assembly of the division septum in bacteria is mediated by several proteins that localize to the division site. One of these, FtsI (also called penicillin-binding protein 3) of Escherichia coli,...
Septal Localization of FtsQ, an Essential Cell Division Protein in Escherichia coli
Chen, Joseph C., Weiss, David S., Ghigo, Jean-Marc, Beckwith, Jon
Septation in Escherichia coli requires several gene products. One of these, FtsQ, is a simple bitopic membrane protein with a short cytoplasmic N terminus, a membrane-spanning segment, and a...
Ghigo, Jean-Marc, Beckwith, Jon
In Escherichia coli, nine essential cell division proteins are known to localize to the division septum. FtsL is a 13-kDa bitopic membrane protein with a short cytoplasmic N-terminal domain, a...
Debarbieux, Laurent, Beckwith, Jon
Escherichia coli thioredoxin 1 has been characterized in vivo and in vitro as one of the most efficient reductants of disulfide bonds. Nevertheless, under some conditions, thioredoxin 1 can also act...
Boyd, Dana, Weiss, David S., Chen, Joseph C., Beckwith, Jon
We describe a simple system for reversible, stable integration of plasmid-borne genes into the Escherichia coli chromosome. Most ordinary E. coli strains and a variety of pBR322-derived...
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA
Kadokura, Hiroshi, Beckwith, Jon
Protein disulfide bond formation in Escherichia coli is catalyzed by the periplasmic protein DsbA. A cytoplasmic membrane protein DsbB maintains DsbA in the oxidized state by transferring electrons...
Katzen, Federico, Deshmukh, Meenal, Daldal, Fevzi, Beckwith, Jon
Modular organization of proteins has been postulated as a widely used strategy for protein evolution. The multidomain transmembrane protein DsbD catalyzes the transfer of electrons from the cytoplasm...
Haebel, Peter W., Goldstone, David, Katzen, Federico, Beckwith, Jon, Metcalf, Peter
The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDα) of...
We describe the further utilization of a genetic screen that identifies mutations defective in the assembly of proteins into the Escherichia coli cytoplasmic membrane. The screen yielded mutations in...
Chen, Joseph C., Minev, Michael, Beckwith, Jon
FtsQ, a 276-amino-acid, bitopic membrane protein, is one of the nine proteins known to be essential for cell division in gram-negative bacterium Escherichia coli. To define residues in FtsQ critical...
Katzen, Federico, Beckwith, Jon
The central hydrophobic domain of the membrane protein DsbD catalyzes the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. Two cysteine residues embedded in...
Schierle, Clark F., Berkmen, Mehmet, Huber, Damon, Kumamoto, Carol, Boyd, Dana, Beckwith, Jon
The Escherichia coli cytoplasmic protein thioredoxin 1 can be efficiently exported to the periplasmic space by the signal sequence of the DsbA protein (DsbAss) but not by the signal sequence of...
FtsL, an Essential Cytoplasmic Membrane Protein Involved in Cell Division in Escherichia coli
Guzman, Luz-Maria, Barondess, James J., Beckwith, Jon
We have identified a gene involved in bacterial cell division, located immediately upstream of the ftsI gene in the min 2 region of the Escherichia coli chromosome. This gene, which we named ftsL,...
Deletion of the Escherichia coli crp Gene
Sabourin, Dennis, Beckwith, Jon
Spontaneous crp mutants Escherichia coli were selected from a strain that does not require 3′,5′-cyclic adenosine monophosphate for CAP activity. Several deletions of the crp gene were...
Cyclic Adenosine Monophosphate-Independent Mutants of the Lactose Operon of Escherichia coli
Arditti, Rita, Grodzicker, Terri, Beckwith, Jon
In Escherichia coli the transcription of the lactose operon, like other catabolite-sensitive operons, requires catabolite gene activator protein and 3′,5′-cyclic adenosine monophosphate in...
Brickman, Edith, Soll, Larry, Beckwith, Jon
Sixty-two spontaneous mutations have been characterized which reduce the level of expression of catabolite-sensitive operons. These mutations appear to affect either the crp (catabolite gene...
Mechanism of Activation of Catabolite-Sensitive Genes: A Positive Control System*
Zubay, Geoffrey, Schwartz, Daniele, Beckwith, Jon
Catabolite repression is defined as the inhibition of enzyme induction by glucose or related substances. In the bacterium E. coli, the effect of glucose appears to be due to a lowering of the cyclic...
Ortenberg, Ron, Gon, Stéphanie, Porat, Amir, Beckwith, Jon
A strain of Escherichia coli missing three members of the thioredoxin superfamily, thioredoxins 1 and 2 and glutaredoxin 1, is unable to grow, a phenotype presumed to be due to the inability of cells...
Goehring, Nathan W., Gueiros-Filho, Frederico, Beckwith, Jon
Cell division in Escherichia coli requires the recruitment of at least 10 essential proteins to the bacterial midcell. Recruitment of these proteins follows a largely linear dependency pathway in...
Kadokura, Hiroshi, Nichols, Lorenzo, Beckwith, Jon
The DsbA-DsbB pathway introduces disulfide bonds into newly translocated proteins. Conversion of the conserved cis proline 151 of DsbA to several hydrophilic residues results in accumulation of mixed...
Huber, Damon, Boyd, Dana, Xia, Yu, Olma, Michael H., Gerstein, Mark, Beckwith, Jon
We have previously reported that the DsbA signal sequence promotes efficient, cotranslational translocation of the cytoplasmic protein thioredoxin-1 via the bacterial signal recognition particle...
A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo
Huber, Damon, Cha, Myoung-il, Debarbieux, Laurent, Planson, Anne-Gaëlle, Cruz, Nelly, López, Gary, ...
Escherichia coli thioredoxin is normally a cytoplasmic protein involved in the reduction of disulfide bonds. However, thioredoxin can be translocated to the periplasm when it is attached to a...
Cho, Seung-Hyun, Beckwith, Jon
The cytoplasmic membrane protein DsbD keeps the periplasmic disulfide isomerase DsbC reduced, using the cytoplasmic reducing power of thioredoxin. DsbD contains three domains, each containing two...
Reply to Hook and Lowden: the definition and implications of genetic discrimination.
Billings, Paul R, Alper, Joseph S, Beckwith, Jon, Barash, Carol I, Natowicz, Marvin R
Gon, Stéphanie, Camara, Johanna E, Klungsøyr, Hege K, Crooke, Elliott, Skarstad, Kirsten, Beckwith, Jon
We present evidence for a complex regulatory interplay between the initiation of DNA replication and deoxyribonucleotide synthesis. In Escherichia coli, the ATP-bound DnaA protein initiates...
Goehring, Nathan W., Petrovska, Ivana, Boyd, Dana, Beckwith, Jon
Cell division in Escherichia coli requires the concerted action of at least 10 essential proteins. One of these proteins, FtsQ, is physically associated with multiple essential division proteins,...
Role for the Nonessential N Terminus of FtsN in Divisome Assembly▿
Goehring, Nathan W., Robichon, Carine, Beckwith, Jon
FtsN, the last essential protein in the cell division localization hierarchy in Escherichia coli, has several peculiar characteristics, suggesting that it has a unique role in the division process...
Contribution of the FtsQ Transmembrane Segment to Localization to the Cell Division Site▿
Scheffers, Dirk-Jan, Robichon, Carine, Haan, Gert Jan, Den Blaauwen, Tanneke, Koningstein, Gregory, Van Bloois, Edwin, ...
The Escherichia coli cell division protein FtsQ is a central component of the divisome. FtsQ is a bitopic membrane protein with a large C-terminal periplasmic domain. In this work we investigated the...
Sevier, Carolyn S., Kadokura, Hiroshi, Tam, Vincent C., Beckwith, Jon, Fass, Deborah, Kaiser, Chris A.
Three different classes of thiol-oxidoreductases that facilitate the formation of protein disulfide bonds have been identified. They are the Ero1 and SOX/ALR family members in eukaryotic cells, and...
Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility
Cho, Seung-Hyun, Porat, Amir, Ye, Jiqing, Beckwith, Jon
The membrane-embedded domain of the unusual electron transporter DsbD (DsbDβ) uses two redox-active cysteines to catalyze electron transfer between thioredoxin-fold polypeptides on opposite sides of...
Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways
Faulkner, Melinda J., Veeravalli, Karthik, Gon, Stéphanie, Georgiou, George, Beckwith, Jon
In Escherichia coli, the glutathione/glutaredoxin and thioredoxin pathways are essential for the reduction of cytoplasmic protein disulfide bonds, including those formed in the essential enzyme...
Dutton, Rachel J., Boyd, Dana, Berkmen, Mehmet, Beckwith, Jon
Protein disulfide bond formation contributes to the folding and activity of many exported proteins in bacteria. However, information about disulfide bond formation is limited to only a few bacterial...
Robichon, Carine, King, Glenn F., Goehring, Nathan W., Beckwith, Jon
Bacterial cell division is mediated by a set of proteins that assemble to form a large multiprotein complex called the divisome. Recent studies in Bacillus subtilis and Escherichia coli indicate that...
Gonzalez, Mark D., Beckwith, Jon
Cell division in bacteria requires the coordinated action of a set of proteins, the divisome, for proper constriction of the cell envelope. Multiple protein-protein interactions are required for...