Sequence of ptb1, a Gene for the β subunit of the type-II geranylgeranyltransferase from the fission yeast Schizosaccharomyces pombe

Godfrey, Rita E.; Davey, John

doi:10.1002/(sici)1097-0061(199604)12:5<479::aid-yea926>3.0.co;2-p

Cited by 3 publications

(1 citation statement)

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“…Thus, we have now identified all subunit genes for GGTase I and FTase in S. pombe . Together with the previously described ptb1 + gene that encodes the β‐subunit of GGTase II (Godfrey and Davey, 1996), most S. pombe genes encoding prenyltransferases have been identified. This establishes S. pombe as a particularly attractive system to study protein prenylation.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the geranylgeranyl transferase type I from Schizosaccharomyces pombe

Arellano

Coll

Yang

et al. 1998

Molecular Microbiology

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SummaryThe Schizosaccharomyces pombe cwg2 þ gene encodes the ␤-subunit of geranylgeranyl transferase I (GGTase I), which participates in the post-translational C-terminal modification of several small GTPases, allowing their targeting to the membrane. Using the two-hybrid system, we have identified the cwp1 þ gene that encodes the ␣-subunit of the GGTase I. cwp1p interaction with cwg2p was mapped to amino acids 1-244 or 137-294 but was not restricted to amino acids 137-244. The genomic cwp1 þ was isolated and sequenced. It has two putative open reading frames of 677 and 218 bp, separated by a 51 bp intron. The predicted amino acid sequence shows significant similarity to GGTase I ␣-subunits from different species. However, complementation of Saccharomyces cerevisiae ram2-1 mutant by overexpressing the cwp1 þ gene was not possible. Expression of both cwg2 þ and cwp1 þ in Escherichia coli allowed 'in vitro' reconstitution of the GGTase I activity. S. pombe cells expressing the mutant enzyme containing the cwg2-1 mutation do not grow at 37ЊC, but the growth defect can be suppressed by the addition of sorbitol. Actin immunostaining of the cwg2-1 mutant strain grown at 37ЊC showed an abnormal distribution of actin patches. The cwg2-1 mutation was identified as a guanine to adenine substitution at nucleotide 604 of the coding region, originating the change A202T in the cwg2p. Deletion of the cwg2 gene is lethal; ⌬cwg2 spores can divide two or three times before losing viability. Most cells have aberrant morphology and septation defects. Overexpression of the rho1G15VC199R double-mutant allele in S. pombe caused loss of polarity but was not lethal and did not render the (1-3)␤-D-glucan synthase activity independent of GTP. Therefore, geranylgeranylation of rho1p is required for the appropriate function of this GTPase.

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Section: Discussionmentioning

confidence: 99%