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Biomedical subjects

S Cutting

Publications and source records attributed to S Cutting.

At least 19 recordsLinked to original sources
PubMed2001

Adult-onset idiopathic generalized epilepsy: clinical and behavioral features.

PURPOSE: To identify and define clinical and behavioral features of patients with adult-onset idiopathic generalized epilepsy (IGE). METHODS: We reviewed the charts of 313 IGE patients at the NYU Comprehensive Epilepsy Center over the past 5 years to identify patients with adult onset (18 years old or older). We excluded patients with childhood or adolescent symptoms that suggested absence, myoclonic, or tonic-clonic seizures, as well as those with a history of significant head injury or other known causes of localization-related epilepsy. RESULTS: Forty-two (13.4%) patients had a clear onset of IGE in adulthood; average age of onset was early 20s (mean, 23.8 years; range, 18-55 years). Twenty-one patients had adult myoclonic epilepsy (AME, 50%), and three had generalized tonic-clonic seizures on awakening (GTCS-A, 7%). More than two thirds (n=30) are well controlled with current antiepileptic drugs (AEDs), and almost 90% are currently employed (n=37). One third were diagnosed and treated for mental disorders, including depression (n=12), anxiety (n=7), obsessive-compulsive personality disorder (n=2), and postictal psychosis (n=1). CONCLUSIONS: Adult-onset IGE is associated with a good prognosis. An association may exist between psychological disorders, psychotropic medication, and level of seizure control in adults with IGE.

Adolescent↗
PubMed2000

BofC negatively regulates SpoIVB-mediated signalling in the Bacillus subtilis sigmaK-checkpoint.

The BofC protein acts negatively on intercompartmental signalling of pro-sigma(K) processing in the sigma(K)-checkpoint of Bacillus subtilis. Signalling is brought about by the SpoIVB protein, which is synthesized in the forespore and initiates proteolytic processing of pro-sigmaK to its mature and active form in the opposed mother cell chamber of the developing cell. We have shown here that BofC, like SpoIVB, is secreted across the inner forespore membrane and, from the analysis of a bofC deletion and insertion mutant, is likely to interact with SpoIVB. In the absence of BofC, the amount of SpoIVB found in sporulating cells is substantially reduced, although SpoIVB is still able to activate proteolysis of pro-sigma(K). Conversely, in the absence of SpoIVB, the levels of BofC accumulate suggesting that the fate of each molecule is dependent upon their mutual interaction. Our results suggest that BofC could maintain SpoIVB in a stable but inactive form. Supporting this, we have shown that overproduction of BofC inhibits SpoIVB autoproteolysis and leads to a delay in proteolytic cleavage of pro-sigma(K). Based on our work here, we have proposed a model for BofC's functional role in intercompartmental signalling.

Bacillus subtilis↗
PubMed1997

Characterization of csgA, a new member of the forespore-expressed sigmaG-regulon from Bacillus subtilis.

A new locus, csgA, has been identified in a search for developmental genes transcribed by E sigmaG in Bacillus subtilis. csgA has the potential to encode three small proteins, CsgAA, CsgAB and CsgAC. The latter two would be encoded by overlapping ORFs. csgA is expressed in the spore chamber of the differentiating cell and is under the control of sigmaG and the transcriptional regulatory protein SpoVT. Mutation of csgA did not affect spore formation but produced a subtle defect in the ability of the germinating spore to resume vegetative growth.

Amino Acid Sequence↗
PubMed1997

SpoIVB has two distinct functions during spore formation in Bacillus subtilis.

The Bacillus subtilis SpoIVB protein is a critical component of the intercompartmental signal-transduction pathway that activates the sigma factor, delta K, in the mother cell of the sporulating cell. SpoIVB, synthesized in the forespore chamber, must act across two layers of phospholipid membrane to facilitate proteolytic processing of inactive pro-delta K to active delta K. We have used a genetic approach to dissect SpoIVB function and found that this protein has two distinct developmental functions. One function is that of intercompartmental signalling of pro-delta K processing. The other role is essential to spore formation and is illustrated by mutations of SpoIVB which allow cell-cell signalling of pro-delta K processing but prevent the formation of viable spores. Using localized and site-specific mutagenesis we have identified a functional domain of SpoIVB that is involved in its non-signalling role.

Bacillus subtilis↗
PubMed1997

SpoVM, a small protein essential to development in Bacillus subtilis, interacts with the ATP-dependent protease FtsH.

The spoVM gene encodes a 26-amino-acid polypeptide that is essential for spore formation in Bacillus subtilis. A transposon insertion within the spoVM open reading frame has been shown to encode a chimeric protein which is biologically inactive and produces a phenotype identical to that of a deletion and insertion mutation. A genetic approach was used to identify possible interacting proteins, and the membrane-bound FtsH protease was identified. Mutations in ftsH suppressed the sporulation defect of certain spoVM mutants but not others. However, production of the mother cell sigma factors, sigmaE and sigmaK, was abnormal in the suppressed strains, and mutations in either spoVM or ftsH alone impaired sigma factor production and sporulation gene expression. Using FtsH purified from Escherichia coli, we demonstrated that in vitro (i) SpoVM inhibits FtsH protease activity and (ii) SpoVM is a substrate for the FtsH protease. We propose that during sporulation, SpoVM serves as a competitive inhibitor of FtsH activity. This interaction appears to be important for completion of the prespore engulfment step of sporulation, based on the phenotype of certain spoVM ftsH double mutants.

ATP-Dependent Proteases↗
PubMed1996

A compartmentalized regulator of developmental gene expression in Bacillus subtilis.

We have identified a new Bacillus subtilis gene, spoVT, whose gene product is homologous to the transcriptional regulator AbrB and serves as a regulator of E sigmaG-controlled gene expression. SpoVT acts both positively and negatively in controlling sigmaG-dependent gene expression, providing an additional level of refinement to forespore gene regulation and feedback control of spoIIIG expression.

Amino Acid Sequence↗
PubMed1995

Transcription of spoIVB is the only role of sigma G that is essential for pro-sigma K processing during spore formation in Bacillus subtilis.

Activation of pro-sigma K processing in the mother cell at late stages of sporulation in Bacillus subtilis requires the presence of active sigma G in the forespore. Placing the spoIVB gene under the control of sigma F, the early forespore transcription factor, allows sigma K to become active in the absence of sigma G. Therefore, transcription of spoIVB is the only role of sigma G that is essential for the signaling pathway between sigma G and sigma K.

Bacillus subtilis↗
PubMed1995

An additional GerE-controlled gene encoding an abundant spore coat protein from Bacillus subtilis.

We describe the identification and characterization of a gene, herein designated cotG, encoding an abundant coat protein from the spores of Bacillus subtilis. The cotG open reading frame is 195 codons in length and is capable of encoding a polypeptide of 24 kDa that contains nine tandem copies of the 13-amino-acid long, approximately repeated sequence H/Y-K-K-S-Y-R/C-S/T-H/Y-K-K-S-R-S. cotG is located at 300 degrees on the genetic map close to another coat protein gene, cotB. The cotG and cotB genes are in divergent orientation and are separated by 1.3 kb. Like the promoter for cotB, the cotG promoter is induced at a late stage of sporulation under the control of the RNA polymerase sigma factor sigma K and the DNA-binding protein GerE. The -10 and -35 nucleotide sequences of the cotG promoter resemble those of other promoters recognized by sigma K-containing RNA polymerase, and centered 70 bp upstream of the apparent start site is a sequence that matches the consensus binding site for GerE. Spore coat proteins from a newly constructed cotG null mutant lack not only CotG but also CotB, a finding that suggests that CotG may be a morphogenetic protein that is required for the incorporation of CotB into the coat.

Amino Acid Sequence↗
PubMed1995

Sporulation protein SpoIVFB from Bacillus subtilis enhances processing of the sigma factor precursor Pro-sigma K in the absence of other sporulation gene products.

Processing of inactive pro-sigma K to active sigma K in the mother cell compartment of sporulating Bacillus subtilis is governed by a signal transduction pathway emanating from the forespore and involving SpoIVFB in the mother cell. Coexpression of spoIVFB and sigK (encoding pro-sigma K) genes in growing B. subtilis or Escherichia coli enhanced pro-sigma K processing in the absence of other sporulation-specific gene products. The simplest explanation of these results is that SpoIVFB is a protease that processes pro-sigma K.

Bacillus subtilis↗
PubMed1993

An unusually small gene required for sporulation by Bacillus subtilis.

We report the cloning and characterization of an unusually small gene called spoVM whose product is required for normal formation of the cortex and coat during sporulation in Bacillus subtilis. The spoVM gene is adjacent to, and in convergent orientation with, the B. subtilis homologue to the Escherichia coli gene for ribosomal protein L28. The spoVM open reading frame is only 26 codons in length and is capable of encoding a polypeptide of 3 kDa. The short length of spoVM was verified by means of complementation experiments with wild-type and deletion-mutated copies of the open reading frame and by engineering the synthesis of the spoVM gene product in E. coli. Transcription of spoVM was induced during the second hour of sporulation (approximately stage II) by the appearance of the sporulation RNA polymerase sigma factor, sigma E. Efficient transcription of spoVM additionally required the action of the sporulation DNA-binding protein SpoIIID. Because spoVM was not strongly required for the transcription of several genes expressed at late times in development, its protein product is likely to play a morphogenetic rather than a regulatory role in sporulation.

Amino Acid Sequence↗
PubMed1992

Characterization of bofA, a gene involved in intercompartmental regulation of pro-sigma K processing during sporulation in Bacillus subtilis.

Sporulating cells of the gram-positive bacterium Bacillus subtilis are partitioned into two cellular compartments called the mother cell and the forespore. Gene expression in the mother cell and the forespore is regulated differentially by the compartment-specific transcription factors sigma K and sigma G, respectively. Gene expression between the two compartments is also coordinated by a signal transduction pathway that couples the activation of sigma K (by processing of its inactive precursor pro-sigma K) in the mother cell to sigma G-directed gene expression in the forespore. To dissect the signal transduction pathway genetically, we previously isolated bypass of forespore mutations at loci called bofA and bofB that relieve the dependence of pro-sigma K processing on the action of sigma G. bofB mutations were previously shown to be allelic to the two-cistron sporulation operon spoIVF, which encodes the pro-sigma K-processing enzyme or its regulator. We now report that bofA mutations are located in a small open reading frame of 87 codons that encodes a putative integral membrane protein with three potential membrane-spanning domains. The possibility is discussed that BofA and the SpoIVF proteins form a heteromeric complex in the mother cell membrane that surrounds the forespore and that this complex mediates the intercompartmental coupling of pro-sigma K processing to events in the forespore.

Amino Acid Sequence↗
PubMed1992

Characterization of the Bacillus subtilis sporulation gene spoVK.

The sporulation gene spoVK of Bacillus subtilis was cloned by use of the insertional mutation spoVK::Tn917 omega HU8. The spoVK gene was shown to be the site of an incorrectly mapped mutation called spoVJ517. Thus, a separate spoVJ gene as defined by the 517 mutation does not exist and is instead identical with spoVK.

Bacillus subtilis↗
PubMed1991

Sporulation operon spoIVF and the characterization of mutations that uncouple mother-cell from forespore gene expression in Bacillus subtilis.

During the process of endospore formation in Bacillus subtilis the appearance of the mother-cell transcription factor sigma K by conversion from its inactive precursor pro-sigma K is coupled to events under the control of the forespore transcription factor sigma G. This intercompartmental coupling is believed to be mediated by the products of a sporulation locus called spoI V F because certain bypass-of-forespore (bof) mutations that map at the spoI V F locus relieve the dependence of pro-sigma K processing on the action of sigma G in the forespore. We now report that spoI V F is a two-cistron operon whose transcription is under the control of the sporulation transcription factor sigma E and whose products are likely to be integral membrane proteins. We show that the products of both the promoter-proximal (spoI V F A) and promoter-distal (spoI V F B) cistrons are required for spore formation at 37 degrees C, but that the spoI V F A gene product is dispensable at 30 degrees C. The bypass-of-forespore mutations are located at the extreme 3' end of the spoI V F A cistron, one such mutation causing a proline to serine substitution eight residues from the COOH terminus of SpoIVFA and another (a nonsense mutation) causing the absence of the terminal six amino acid residues of the protein. We also show that at a permissive temperature for spore formation spoI V F A null mutants exhibit a bypass-of-forespore phenotype. We hypothesize that SpoIVFA functions positively in stabilizing SpoIVFB, which we propose is thermolabile in the absence of the promoter-proximal gene product, and negatively in inhibiting the action of SpoIVFB. A model for intercompartmental coupling is presented in which SpoIVFB promotes pro-sigma K processing in response to a signal from the forespore that relieves or otherwise counteracts the inhibitory effect of SpoIVFA on SpoIVFB.

Amino Acid Sequence↗
PubMed1991

Forespore-specific transcription of a gene in the signal transduction pathway that governs Pro-sigma K processing in Bacillus subtilis.

We present studies on the regulation of a developmental gene (spoIVB) whose product is required at a late stage of morphogenesis during the process of sporulation in Bacillus subtilis. Earlier work implicated the spoIVB gene product in a signal-transduction pathway that governs the conversion of pro-sigma K to the mature and active form of the mother cell sigma factor, sigma K, in response to a signal generated within the forespore chamber of the sporangium. We now show that (1) spoIVB is induced at the engulfment stage of sporulation, (2) this transcription is restricted to the forespore, and (3) spoIVB is under the direct control of the forespore sigma factor sigma G. The discovery that spoIVB is a forespore-expressed gene suggests that the spoIVB gene product, or a developmental event under its control, triggers the processing of pro-sigma K and thereby mediates the coupling of sigma K-directed gene expression in the mother cell to sigma G-directed gene expression in the forespore. We also show that spoIVB transcription is partially dependent on the action of the mother cell regulatory gene spoIIID, a finding that suggests that the transcription of certain forespore-expressed genes is influenced by events in the mother cell.

Bacillus subtilis↗
PubMed1991

Gene encoding two alkali-soluble components of the spore coat from Bacillus subtilis.

We report the cloning and characterization of a gene called cotF from Bacillus subtilis that encodes alkali-soluble polypeptides of 5 and 8 kDa that are components of the spore coat. The 5- and 8-kDa polypeptides are generated by proteolytic cleavage of the primary product of the cotF gene, which is 160 codons in length and is capable of encoding a polypeptide of 19 kDa. Amino acid sequence analysis indicates that the 5-kDa species is derived from the NH2-terminal portion of the primary gene product and that the 8-kDa species is derived from the COOH-terminal portion. A mutant bearing an in vitro-constructed cotF null mutation produced normal-looking spores that contained an apparently complete set of coat proteins except for the absence of the 5- and 8-kDa polypeptides. The map position of cotF is 349 degrees. Transcription of cotF commenced coincidently (during h 6 of sporulation) with genes known to be under the control of sporulation transcription factor sigma kappa.

Amino Acid Sequence↗
PubMed1990

A forespore checkpoint for mother cell gene expression during development in B. subtilis.

Gene expression in the mother cell compartment of sporulating cells of B. subtilis is partly governed by the mother cell RNA polymerase sigma factor sigma K. Paradoxically, sigma K-directed gene expression also depends on sigma G, the product of the forespore compartment regulatory gene spoIIIG, and on other forespore regulatory proteins. We now identify mutations in the genes bofA and bofB that relieve the dependence of mother cell gene expression on forespore regulatory proteins but not on sigma K. We establish that the dependence of mother cell gene expression on the forespore regulatory proteins is mediated at the level of the conversion of pro-sigma K to its mature, active form. We propose that the bofA and/or bofB proteins govern this conversion in response to a signal generated by the forespore. Activation of pro-sigma K could be a checkpoint for coordinating gene expression between the mother cell and forespore compartments of the developing sporangium.

Bacillus subtilis↗
PubMed1989

Regulatory studies on the promoter for a gene governing synthesis and assembly of the spore coat in Bacillus subtilis.

gerE is a regulatory gene of Bacillus subtilis that governs the synthesis and assembly of the spore coat and is required for the production of spores that are lysozyme-resistant and germination-proficient. We report the identification of the promoter for gerE and studies on the regulation of its expression. We show that gerE is switched on at the fourth hour of sporulation (stage-V) and that this expression is restricted to the mother-cell chamber of the sporangium. Dependency studies in which the level of gerE expression was measured in 36 different developmental mutants indicate that efficient expression of gerE requires the products of almost all spo0-IV genes tested as well as certain spoV genes. On the basis of its time of induction, compartmentalization of expression and pattern of dependence on other spo genes, gerE is inferred to be regulated co-ordinately with the previously studied spore coat protein gene cotA. gerE and cotA may be members of a developmental regulon of genes whose products are involved in the assembly of the spore coat.

Bacillus subtilis↗