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Corresponding author: Charles S. Hoffman, Department of Biology, Boston College, Higgins Hall 315, Chestnut Hill, MA 02467., hoffmacs{at}bc.edu (E-mail)
Communicating editor: P. G. YOUNG
 | ABSTRACT |
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 TOP ABSTRACT MATERIALS AND METHODSRESULTSDISCUSSIONLITERATURE CITED |
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Fission yeast adenylate cyclase is activated by the gpa2 G
subunit of a heterotrimeric guanine-nucleotide binding protein (G protein). We show that the git5 gene, also required for this activation, encodes a Gß subunit. In contrast to another study, we show that git5 is not a negative regulator of the gpa1 G involved in the pheromone response pathway. While 43% identical to mammalian Gß's, the git5 protein lacks the amino-terminal coiled-coil found in other Gß subunits, yet the gene possesses some of the coding capacity for this structure 5' to its ORF. Although both gpa2 (G) and git5 (Gß) are required for adenylate cyclase activation, only gpa2 is needed to maintain basal cAMP levels. Strains bearing a git5 disruption are derepressed for fbp1 transcription and sexual development even while growing in a glucose-rich environment, although fbp1 derepression is half that observed in gpa2 deletion strains. Multicopy gpa2 partially suppresses the loss of git5, while the converse is not true. These data suggest that Gß is required for activation of adenylate cyclase either by promoting the activation of G or by independently activating adenylate cyclase subsequent to G stimulation as seen in type II mammalian adenylate cyclase activation.
HETEROTRIMERIC G proteins are composed of , ß, an 
subunits and regulate many eukaryotic signal transduction pathways. G protein activation involves a receptor-stimulated GDP to GTP exchange of the guanine nucleotide bound to the G subunit, followed by the release of the G subunit from the Gß dimer (
subunit alone regulates the activity of effector molecules directly; however, this model has undergone considerable revision, as effectors that are stimulated by Gß alone, by G and Gß acting independently, or by G in concert with Gß have been identified (
Two genes from the fission yeast Schizosaccharomyces pombe that encode G subunits have been identified. The gpa1 gene encodes a positive regulator of the pheromone-induced mating pathway ( subunits have been identified previously in S. pombe.
S. pombe regulates intracellular cAMP levels in response to nutritional signals (
Previously, we identified eight git (glucose insensitive transcription) genes by mutations that confer constitutive fbp1 transcription ( gene gpa2 (
| MATERIALS AND METHODS |
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| TOPABSTRACTMATERIALS AND METHODSRESULTSDISCUSSIONLITERATURE CITED |
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Yeast strains and growth media:
Yeast strains used are listed in Table 1. Genetic nomenclature for S. pombe follows rules proposed by
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Standard rich media yeast extract agar and yeast extract liquid (
Recombinant DNA methodology:
Standard recombinant DNA techniques, including DNA restriction digests, ligations, and Escherichia coli transformations, were performed according to
Cloning of git5+:
Constitutive transcription of thefbp1-ura4+ reporter due to the git5-311 mutant allele in CHP311 results in a 5-FOA-sensitive phenotype. The git5+ gene carried on plasmid pMP1 was cloned by its ability to confer 5-FOA resistance upon transformation of strain CHP311 with a S. pombe genomic library (
Plasmid pMP1 was linearized with BglII and was integrated into strain FWP112 (git+;
Plasmid pSL10 carrying a cDNA clone of git5+ was identified from a 
ZAP II S. pombe cDNA library (
Quantitative oligonucleotide-directed S1 analysis:
Oligonucleotide-directed S1 was performed as described previously (
Construction of a git5
gene disruption:
The git5 gene was disrupted by replacing a BamHI to XbaI fragment including codons 99–152 of the git5 ORF with a 1.9-kb BglII to XbaI DNA fragment carrying the his7+ gene (; resulting in strain CHP469). The git5-1::his7+ disruption (git5) was then crossed into strains carrying thefbp1-ura4+ reporter and was shown to confer a 5-FOA-sensitive phenotype, similar to that of git5 mutant strains. Complementation tests with other git mutant strains were performed as previously described ( strain with a git5 point mutant places the git5 allele in the git5 complementation group.
Subcloning of the git5 ORF:
A 1.4-kb SspI fragment from plasmid pSL10, carrying the git5 ORF, was blunt-end ligated into the SmaI site of plasmid pART1 (
High-copy-number suppression analyses:
High-copy-number suppression was determined by transforming host strains to Leu+ with plasmids expressing gpa2+ or git5+, along with empty-vector controls. Transformants were tested for sensitivity or resistance to 5-FOA, as an indication of fbp1-ura4+ transcription, and assayed for ß-galactosidase activity expressed from the fbp1-lacZ reporter as described previously (
cAMP assays:
Intracellular cAMP levels were measured in glucose-starved cells (basal level) and in the same cultures 1 min after exposure to 100 mM glucose as previously described (
| RESULTS |
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| TOPABSTRACTMATERIALS AND METHODSRESULTSDISCUSSIONLITERATURE CITED |
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Cloning and nucleotide sequence of the git5+ gene:
The git5+ gene was cloned from an S. pombe genomic library by its ability to complement a git5 mutation in strain CHP311 (see MATERIALS AND METHODS). Homologous integration of this plasmid and a subsequent linkage analysis demonstrated that the clone carries the git5+ gene, rather than a high-copy-number suppressor of the git5-311 mutation. Our DNA sequence analysis in the region of plasmid pMP1 that carries the git5 complementing activity (accession no. AF092102) reveals that git5+ gene is the same as gpb1 (
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Analysis and subcloning of the git5 ORF:
The putative 305-residue git5 product is ~44% identical and 62% similar to Gß subunits from other organisms (Fig 2). However, for the 16 residues identified as contacting the G subunit from a crystal structure analysis (
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The most unusual characteristic of the predicted 305-residue product is the absence of 36 residues at the amino terminus relative to other members of this family (Fig 2). This region of other Gß subunits forms a coiled-coil that appears to be required for the formation of the Gß dimer ( subunit. Modeling of the 305-residue git5 protein predicts only 14 residues preceding the ß propeller, suggesting a loss of 15 G contact residues (data not shown). Of the remaining 34 G contact residues of bosGb1, 19 (56%) are conserved in git5 (Fig 2). However, the location of these conserved residues is strikingly restricted to the central blades of the Gß that contact G. In blades 5, 6, 7, and 1, 16 of 21 (76%) G contact residues are conserved, while in blades 2 and 4, as well as the 14 residues preceding the ß propeller, only 3 of 13 (23%) G contact residues are conserved.
The git5 gene contains a single 305-codon ORF:
The coding capacity of the DNA immediately upstream of the git5 ORF displays characteristics of a classical Gß subunit amino terminus, as residues defined by the 9 "codons" prior to the start codon are highly conserved with respect to other Gß subunits (Fig 2). In addition, the sequence TAG, which commonly identifies a 3' splice site in S. pombe, is present 3' to the in-frame STOP codon preceding the git5 ORF but 5' to these codons. This led us to assume that one or more exons must be present 5' to this ORF, such that the true git5 product possesses a standard amino-terminal coiled-coil. However, several lines of evidence suggest that there is no splicing and that the 305-codon ORF encodes the complete and functional git5 product.
We have cloned a cDNA copy of git5 (see MATERIALS AND METHODS) and found its sequence to be colinear to the genomic DNA. The cloned sequence in plasmid pSL10 initiates 122 bp upstream from the start codon of the 305-residue ORF. The cDNA sequenced in the gbp1 study (
We have looked directly for evidence of splicing at the 5' end of the git5 ORF by oligonucleotide-directed S1 analysis. A 56-nucleotide (nt) probe complementary to the git5 transcript and extending past the in-frame STOP codon preceding the ORF was used both to measure levels of git5 transcription and to detect splice junctions within this region. The probe terminates in 4 nt that are not complementary to the git5 sequence. End-labeled probe was hybridized to RNA from cells grown under repressing and derepressing conditions and treated with exonuclease S1 to degrade any unannealed probe, along with single-stranded portions of the annealed probe. The appearance of a 52-nt protected fragment indicates that git5 transcription initiates upstream from the region complementary to this probe (Fig 3A and Fig B). An overexposed S1 analysis (Fig 3B) shows that the UAG sequence in this region of the mRNA does not serve as a 3' splice site. If such splicing occurred, it would have produced a transcript that only protects 29 nt at the 5' end of the probe. In addition, the ratio of the git5-specific product to a his3-specific product that serves as a loading control reveals a modest increase in git5 transcription under derepressing conditions (Fig 3A).
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To test whether the 305-codon ORF encodes a functional git5 protein, we subcloned the 1.4-kb SspI fragment encompassing this ORF from pSL10 into the pART1 expression vector. Both plasmids pSL11 and pSL12, which carry this fragment in either orientation relative to the vector-provided promoter, complement git5 mutations as they restore glucose repression of fbp1 transcription to the same degree as the original genomic clone (Fig 4 and Table 2), although pSL11 (expressing git5 from the plasmid-borne adh promoter) reduces the general growth rate of transformants. The ability of pSL12 to complement suggests that transcription must also occur from ars1 adjacent to the cloning polylinker to allow transcription of git5. Since these subclones separate the git5 ORF from all upstream git5 sequences including any other possible start codons, the product of this single exon is functional.
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Disruption of git5 confers phenotypes associated with a defect in glucose monitoring, but not pheromone signaling:
Disruption of the git5 ORF (git5; see MATERIALS AND METHODS) confers Git- mutant phenotypes, including elevated fbp1-lacZ expression in cells grown under glucose-rich conditions (Table 2) and 5-FOA-sensitive growth due to constitutive expression of the fbp1-ura4+ reporter (Fig 4; strain CHP477 carrying empty vector). Complementation analyses place this gene disruption in the git5 complementation group, as a git5-75/git5 diploid strain displays the Git- 5-FOA-sensitive phenotype (data not shown).
The git5 disruption also stimulates conjugation and sporulation of an h90 homothallic strain growing under nutrient-rich conditions that can be suppressed by exogenous cAMP, similar to the phenotype of a gpa2 strain (Fig 5). Derepression of sexual development was also attributed to the null allele in the gpb1 study, although the authors of that study concluded that this is due to the activation of the gpa1 protein that positively regulates the pheromone response pathway ( mutants is starvation independent, but not pheromone independent.
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As shown in Fig 6, a heterothallic git5 strain does not produce conjugation tubes when starved in the absence of a mating partner, as is seen in a strain carrying the activated allele of gpa1 (gpa1QL;
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High-copy suppression by gpa2+ and git5+:
While multicopy git5+ expression suppresses git5 point mutations and a git5 deletion, it has no effect upon mutations in the other five genes required for adenylate cyclase activation (gpa2, git1, git3, git7, or git10; data shown for only the gpa2 mutant strain; Fig 4 and Table 2). In contrast to this, gpa2+ (G) overexpression suppresses the mutant phenotypes associated with the git5 disruption (Fig 4 and Table 2). However, the suppression of a git5 deletion by gpa2+ overexpression is only partial compared to suppression by git5+ itself (Table 2), as indicated by the inability of G overexpression to fully repress fbp1-lacZ expression in a git5 mutant strain. This genetic relationship is consistent with a model in which git5 acts in the same heterotrimeric G protein complex as gpa2 (see DISCUSSION).
cAMP levels in gpa2 and git5 disruption strains:
We showed previously that mutations in gpa2 (git8) or in git5 inhibit the glucose-triggered elevation of cAMP levels in fission yeast () mutant, but not in the git5 (Gß) mutant. We show here that deletion of git5 has no effect on basal cAMP levels in strains that either possess or lack the gpa2 gene (Table 3, experiment 1), in agreement with other deletion studies of these two genes (
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| DISCUSSION |
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| TOPABSTRACTMATERIALS AND METHODSRESULTSDISCUSSIONLITERATURE CITED |
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We have shown that the fission yeast git5+ gene encodes a Gß subunit and is identical to the previously cloned gpb1+ gene (
The gpb1 study described the effects of a gbp1 deletion as stimulating conjugation and sporulation under nutrient-rich conditions, which we have also observed. While the authors of that study attributed this to the activation of the gpa1 protein of the pheromone response pathway, our observations are more consistent with a reduction in activation of gpa2 in the glucose-triggered adenylate cyclase activation pathway. If loss of git5/gpb1 activated gpa1, we would expect to see a pheromone-independent stimulation of conjugation as seen by the production of conjugation tubes in a heterothallic strain, similar to that seen in strains carrying an activated allele of gpa1 (gpa1QL;
The data presented here show that the git5 Gß is required for adenylate cyclase activation. The git5 Gß may simply be required for the efficient activation of the gpa2 G, facilitating the delivery of the G to a G-protein-coupled receptor. Alternatively or in addition, git5 may act more directly to stimulate adenylate cyclase as seen for type II mammalian adenylate cyclase ( subunit and the Gß dimer act to stimulate adenylate cyclase in an ordered fashion with the G subunit acting first. Our data to date cannot distinguish between these two possibilities.
As described above, the git5 Gß subunit is unusual in its lack of an amino-terminal coiled-coil found in all other members of this protein family. Complicating this observation is the presence of DNA sequences in the 5' untranslated region of the gene that have the capacity to encode a portion of this domain. At first, we assumed that a splicing event must occur to create a transcript that encodes a standard-length Gß. However, there is only one potential 3' splice junction between an upstream in-frame stop codon and the conserved LVQ codons immediately 5' to the large ORF (Fig 2 and Fig 3B). We show that this site is not utilized in splicing as determined by both DNA sequence analysis of cDNA clones and by the more sensitive oligonucleotide-directed S1 analysis (Fig 3B). Most importantly, a subclone containing only this single ORF is fully functional (Fig 4 and Table 2). Therefore, it appears that the genomic sequence immediately upstream from the 305-codon ORF is an evolutionary remnant from a gene that encoded a standard-length Gß subunit possessing an amino-terminal coiled-coil.
The absence of an amino-terminal coiled-coil in the git5 protein brings into question the existence of a G subunit in this G protein, since binding to G is the major function attributed to this region of Gß ( subunit. The 71-codon ORF present on the cDNA is part of a 72-codon gene whose putative product displays characteristics of a G, including a lysine-rich carboxy terminus and a carboxy-terminal CAAX box (S. LANDRY and C. S. HOFFMAN, unpublished results).
The regulation of S. pombe adenylate cyclase provides us with a genetically pliable model system for the study of G protein signal transduction that is significantly different from that of the well-studied Saccharomyces cerevisiae pheromone response pathway. In this latter system, the Gß dimer is responsible for activation of a mitogen-activated protein kinase cascade, while the G subunit is a negative regulator of pheromone response (
| FOOTNOTES |
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1 Present address: Georgetown University Medical Center, Washington, DC 20007. 
2 Present address: Center of Marine Biotechnology, University of Maryland Biotechnology Institute, Baltimore, MD 21202.
| ACKNOWLEDGMENTS |
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We thank Masayuki Yamamoto for gpa1QL strains and Eva Neer, Fred Winston, and Olaf Nielsen for helpful conversations, suggestions, and questions during the course of this work. We thank Tom Chiles for critical reading of this manuscript and Junona Moroianu for the use of her microscope. This study was supported by National Institutes of Health grant GM46226 to C.S.H.
Manuscript received May 17, 1999; Accepted for publication December 16, 1999.
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