SpoIIAA Governs the Release of the Cell-type Specific Transcription Factor σFFrom its Anti-sigma Factor SpoIIAB

Duncan, Leonard; Alper, Scott; Losick, Richard

doi:10.1006/jmbi.1996.0389

Cited by 110 publications

(157 citation statements)

References 43 publications

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“…4). A comparable result was obtained for SpoIIAA; as a result of substitution of Ser-58 to threonine, sporulation was blocked, although the mutant S58T SpoIIAA was still able to interact with SpoIIAB (44). The phosphorylated serine and threonine residues have in some instances been functionally mimicked by the negatively charged amino acid aspartic acid (43,45,46).…”

Section: Discussionsupporting

confidence: 60%

Structural and Functional Analysis of the C-terminal STAS (Sulfate Transporter and Anti-sigma Antagonist) Domain of the Arabidopsis thaliana Sulfate Transporter SULTR1.2

Rouached

Berthomieu

Kassis

et al. 2005

Journal of Biological Chemistry

110

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The C-terminal region of sulfate transporters from plants and animals belonging to the SLC26 family members shares a weak but significant similarity with the Bacillus sp. anti-anti-sigma protein SpoIIAA, thus defining the STAS domain (sulfate transporter and antisigma antagonist). The present study is a structure/function analysis of the STAS domain of SULTR1.2, an Arabidopsis thaliana sulfate transporter. A three-dimensional model of the SULTR1.2 STAS domain was built which indicated that it shares the SpoIIAA folds. Moreover, the phosphorylation site, which is necessary for SpoIIAA activity, is conserved in the SULTR1.2 STAS domain. The model was used to direct mutagenesis studies using a yeast mutant defective for sulfate transport. Truncation of the whole SULTR1.2 STAS domain resulted in the loss of sulfate transport function. Analyses of small deletions and mutations showed that the Cterminal tail of the SULTR1.2 STAS domain and particularly two cysteine residues plays an important role in sulfate transport by SULTR1.2. All the substitutions made at the putative phosphorylation site Thr-587 led to a complete loss of the sulfate transport function of SULTR1.2. The reduction or suppression of sulfate transport of the SULTR1.2 mutants in yeast was not due to an incorrect targeting to the plasma membrane. Both our three-dimensional modeling and mutational analyses strengthen the hypothesis that the SULTR1.2 STAS domain is involved in protein-protein interactions that could control sulfate transport.

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Section: Discussionsupporting

confidence: 60%

Structural and Functional Analysis of the C-terminal STAS (Sulfate Transporter and Anti-sigma Antagonist) Domain of the Arabidopsis thaliana Sulfate Transporter SULTR1.2

Rouached

Berthomieu

Kassis

et al. 2005

Journal of Biological Chemistry

110

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“…Unfortunately, we have not yet found a means of measuring adenosine nucleotide levels in situ. Meanwhile, Duncan et al (1996) have recently shown that partner switching can also be effected in vitro by addition of a large molar excess of SpoIIAA (Ϸ 20-fold), even in the presence of ATP. Our results now provide evidence for a large increase in nonphosphorylated SpoIIAA in the prespore at about the time that j F becomes active.…”

Section: Discussionmentioning

confidence: 99%

Compartmentalized distribution of the proteins controlling the prespore‐specific transcription factor σ^F of Bacillus subtilis

1996

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Background: Differential gene expression during sporulation in the prespore and mother cell of Bacillus subtilis is dependent on the correct timing and localization of the activity of specific transcription (j) factors. The first j factor activated is j F , which directs gene expression specifically in the prespore compartment. Release of j F activity is tightly controlled through a series of complex interactions involving an anti-j factor, SpoIIAB, an anti-anti-j factor SpoIIAA and a phosphoprotein phosphatase SpoIIE. In vitro studies have shown that SpoIIAB binds to j F , preventing transcription of the j F regulon, and that it can also phosphorylate SpoIIAA, thereby inactivating it. However, nonphosphorylated SpoIIAA can displace j F from SpoIIAB. The SpoIIE phosphatase provides a means of reactivating SpoIIAA-P.

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“…Early in vitro experiments indicated that SpoIIAB bound F in the presence of ATP, whereas it bound SpoIIAA in the presence of ADP (3,44,50). This result suggested that different concentrations of these nucleotides in the two compartments might be responsible for compartmentalization of F activity to the prespore.…”

Section: Mechanisms Of Compartmentalizationmentioning

confidence: 99%

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Hilbert

Piggot

2004

Microbiol Mol Biol Rev

320

432

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Gene expression in members of the family Bacillaceae becomes compartmentalized after the distinctive, asymmetrically located sporulation division. It involves complete compartmentalization of the activities of sporulation-specific sigma factors, σF in the prespore and then σE in the mother cell, and then later, following engulfment, σG in the prespore and then σK in the mother cell. The coupling of the activation of σF to septation and σG to engulfment is clear; the mechanisms are not. The σ factors provide the bare framework of compartment-specific gene expression. Within each σ regulon are several temporal classes of genes, and for key regulators, timing is critical. There are also complex intercompartmental regulatory signals. The determinants for σF regulation are assembled before septation, but activation follows septation. Reversal of the anti-σF activity of SpoIIAB is critical. Only the origin-proximal 30% of a chromosome is present in the prespore when first formed; it takes ≈15 min for the rest to be transferred. This transient genetic asymmetry is important for prespore-specific σF activation. Activation of σE requires σF activity and occurs by cleavage of a prosequence. It must occur rapidly to prevent the formation of a second septum. σG is formed only in the prespore. SpoIIAB can block σG activity, but SpoIIAB control does not explain why σG is activated only after engulfment. There is mother cell-specific excision of an insertion element in sigK and σE-directed transcription of sigK, which encodes pro-σK. Activation requires removal of the prosequence following a σG-directed signal from the prespore

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SpoIIAA Governs the Release of the Cell-type Specific Transcription Factor σFFrom its Anti-sigma Factor SpoIIAB

Cited by 110 publications

References 43 publications

Structural and Functional Analysis of the C-terminal STAS (Sulfate Transporter and Anti-sigma Antagonist) Domain of the Arabidopsis thaliana Sulfate Transporter SULTR1.2

Structural and Functional Analysis of the C-terminal STAS (Sulfate Transporter and Anti-sigma Antagonist) Domain of the Arabidopsis thaliana Sulfate Transporter SULTR1.2

Compartmentalized distribution of the proteins controlling the prespore‐specific transcription factor σ^F of Bacillus subtilis

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

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SpoIIAA Governs the Release of the Cell-type Specific Transcription Factor σFFrom its Anti-sigma Factor SpoIIAB

Cited by 110 publications

References 43 publications

Structural and Functional Analysis of the C-terminal STAS (Sulfate Transporter and Anti-sigma Antagonist) Domain of the Arabidopsis thaliana Sulfate Transporter SULTR1.2

Structural and Functional Analysis of the C-terminal STAS (Sulfate Transporter and Anti-sigma Antagonist) Domain of the Arabidopsis thaliana Sulfate Transporter SULTR1.2

Compartmentalized distribution of the proteins controlling the prespore‐specific transcription factor σF of Bacillus subtilis

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

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Compartmentalized distribution of the proteins controlling the prespore‐specific transcription factor σ^F of Bacillus subtilis