scholarly journals ComEB protein is dispensable for transformation but must be translated for optimal synthesis of ComEC

2020 ◽  
Author(s):  
Micaela De Santis ◽  
Jeanette Hahn ◽  
David Dubnau
Keyword(s):  
Bacillus Subtilis ◽  
Transcriptional Control ◽  
Cytidine Deaminase ◽  
Open Reading Frame ◽  
Common Mechanism ◽  
Its Sequence ◽  
Dna Uptake ◽  
Reading Frame ◽  
Ribosomal Binding Site

We show that the ComEB protein is not required for transformation in Bacillus subtilis, despite its expression from within the comE operon under competence control. We show further that the synthesis of the putative channel protein ComEC is translationally coupled to the upstream comEB open reading frame, so that translation of comEB and a suboptimal ribosomal binding site embedded in its sequence are needed for proper comEC expression. Translational coupling appears to be a common mechanism in three major competence operons for the adjustment of protein amounts independent of transcriptional control, probably ensuring the correct stoichiometries for assembly of the transformation machinery. comEB and comFC respectively encode cytidine deaminase and a protein resembling type 1 phosphoribosyl transferases and we speculate that nucleotide scavenging proteins are produced under competence control for efficient reutilization of the products of degradation of the non-transforming strand during DNA uptake.

The US5 Open Reading Frame of Herpes simplex Virus Type 1 Does Encode a Glycoprotein (gJ)

Intervirology ◽  
1998 ◽  
Vol 41 (2-3) ◽  
pp. 91-97 ◽  
Author(s):  
Homayon Ghiasi ◽  
Anthony B. Nesburn ◽  
Steve Cai ◽  
Steven L. Wechsler
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Simplex Virus

scholarly journals Enhancement of Secretion and Extracellular Stability of Staphylokinase in Bacillus subtilis bywprA Gene Disruption

2000 ◽  
Vol 66 (2) ◽  
pp. 476-480 ◽  
Author(s):  
Sang Jun Lee ◽  
Dong Min Kim ◽  
Kwang Hee Bae ◽  
Si Myung Byun ◽  
Jae Hoon Chung
Keyword(s):  
Bacillus Subtilis ◽  
Gene Disruption ◽  
Therapeutic Potential ◽  
Signal Sequence ◽  
Open Reading Frame ◽  
Expression Plasmid ◽  
Reading Frame ◽  
Extracellular Milieu ◽  
Foreign Proteins

ABSTRACT Staphylokinase (SAK), a polypeptide secreted byStaphylococcus aureus, is a plasminogen activator with a therapeutic potential in thrombosis diseases. A Bacillus subtilis strain which is multiply deficient in exoproteases was transformed by an expression plasmid carrying a promoter and a signal sequence of subtilisin fused in frame with the sak open reading frame. However, the amount of SAK secretion was marginal (45 mg/liter). In contrast, disruption of the wprA gene, which encodes a subtilisin-type protease, strongly promoted the production of SAK in the stationary phase (181 mg/liter). In addition, the extracellular stability of mature SAK was dramatically enhanced. These data indicate a significant role of the wprA gene product in degrading foreign proteins, both during secretion and in the extracellular milieu.

scholarly journals Mutation in yaaT Leads to Significant Inhibition of Phosphorelay during Sporulation in Bacillus subtilis

2002 ◽  
Vol 184 (20) ◽  
pp. 5545-5553 ◽  
Author(s):  
Shigeo Hosoya ◽  
Kei Asai ◽  
Naotake Ogasawara ◽  
Michio Takeuchi ◽  
Tsutomu Sato
Keyword(s):  
Bacillus Subtilis ◽  
Fluorescent Protein ◽  
Early Stage ◽  
Response Regulator ◽  
Significant Inhibition ◽  
Open Reading Frame ◽  
Histidine Kinases ◽  
Reading Frame ◽  
Green Fluorescent ◽  
Sporulation Genes

ABSTRACT In the course of a Bacillus subtilis functional genomics project which involved screening for sporulation genes, we identified an open reading frame, yaaT, whose disruptant exhibits a sporulation defect. Twenty-four hours after the initiation of sporulation, most cells of the yaaT mutant exhibited stage 0 of sporulation, indicating that the yaaT mutation blocks sporulation at an early stage. Furthermore, the mutation in yaaT led to a significant decrease in transcription from a promoter controlled by Spo0A, a key response regulator required for the initiation of sporulation. However, neither the level of transcription of spo0A, the activity of σH, which transcribes spo0A, nor the amount of Spo0A protein was severely affected by the mutation in yaaT. Bypassing the phosphorelay by introducing an spo0A mutation (sof-1) into the yaaT mutant suppressed the sporulation defect, suggesting that the yaaT mutation interferes with the phosphorelay process comprising Spo0F, Spo0B, and histidine kinases. We also observed that mutation of spo0E, which encodes the phosphatase that dephosphorylates Spo0A-P, suppressed the sporulation defect in the yaaT mutant. These results strongly suggest that yaaT plays a significant role in the transduction of signals to the phosphorelay for initiation of sporulation. Micrographs indicated that YaaT-green fluorescent protein localizes to the peripheral membrane, as well as to the septum, during sporulation.

scholarly journals The Bovine Herpesvirus Type 1 UL3.5 Open Reading Frame Encodes a Virion Structural Protein

Virology ◽  
1998 ◽  
Vol 240 (1) ◽  
pp. 76-82 ◽  
Author(s):  
Beate Schikora ◽  
Zhiqiang Lu ◽  
Gerald F. Kutish ◽  
Daniel Rock ◽  
Gábor Magyar ◽  
...  
Keyword(s):  
Bovine Herpesvirus ◽  
Open Reading Frame ◽  
Structural Protein ◽  
Reading Frame ◽  
Herpesvirus Type ◽  
Bovine Herpesvirus Type 1

scholarly journals Proliferation Response to Interleukin-2 and Jak/Stat Activation of T Cells Immortalized by Human T-Cell Lymphotropic Virus Type 1 Is Independent of Open Reading Frame I Expression

1999 ◽  
Vol 73 (11) ◽  
pp. 9642-9649 ◽  
Author(s):  
Nathaniel D. Collins ◽  
Celine D’Souza ◽  
Björn Albrecht ◽  
Michael D. Robek ◽  
Lee Ratner ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Cell Lines ◽  
Virus Type ◽  
Interleukin 2 ◽  
Receptor Expression ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Human T Cell

ABSTRACT Human T-cell lymphotropic virus type 1 (HTLV-1), a complex retrovirus, encodes a hydrophobic 12-kD protein from pX open reading frame (ORF) I that localizes to cellular endomembranes and contains four minimal SH3 binding motifs (PXXP). We have demonstrated the importance of ORF I expression in the establishment of infection and hypothesize that p12I has a role in T-cell activation. In this study, we tested interleukin-2 (IL-2) receptor expression, IL-2-mediated proliferation, and Jak/Stat activation in T-cell lines immortalized with either wild-type or ORF I mutant clones of HTLV-1. All cell lines exhibited typical patterns of T-cell markers and maintained mutation fidelity. No significant differences between cell lines were observed in IL-2 receptor chain (α, β, or γc) expression, in IL-2-mediated proliferation, or in IL-2-induced phosphorylated forms of Stat3, Stat5, Jak1, or Jak3. The expression of ORF I is more likely to play a role in early HTLV-1 infection, such as in the activation of quiescent T cells in vivo.

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