Regulation by low temperatures and anaerobiosis of a yeast gene specifying a putative GPI‐anchored plasma membrane

Donzeau, Mariel; Bourdineaud, Jean‐Paul; Lauquin, Guy J.‐M.

doi:10.1111/j.1365-2958.1996.tb02631.x

Cited by 56 publications

(76 citation statements)

References 44 publications

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“…Studies of several other hypoxic/anaerobic genes including SUT1 (34), GPD2 (50), PAU (51), and DNA1 (52) have demonstrated ROX1p-independent hypoxic/anaerobic induction. Another hypoxic/anaerobic gene, TIR/SRP1, has variably been reported to be ROX1p-independent and ROX1p-dependent (35,37). The identification of a LORE in this study indicates that transcription activation is crucial to the increased expression of certain yeast genes in response to extremely low oxygen tension (versus complete anaerobiosis).…”

Section: Rap1p and Lore-binding Protein(s) (Lbp)-mentioning

confidence: 99%

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Identification and Characterization of a Low Oxygen Response Element Involved in the Hypoxic Induction of a Family ofSaccharomyces cerevisiae Genes

Vasconcelles

Jiang

McDaid

et al. 2001

Journal of Biological Chemistry

106

126

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An organism's ability to respond to changes in oxygen tension depends in large part on alterations in gene expression. The oxygen sensing and signaling mechanisms in eukaryotic cells are not fully understood. To further define these processes, we have studied the ⌬9 fatty acid desaturase gene OLE1 in Saccharomyces cerevisiae. We have confirmed previous data showing that the expression of OLE1 mRNA is increased in hypoxia and in the presence of certain transition metals. OLE1 expression was also increased in the presence of the iron chelator 1,10-phenanthroline. A 142-base pair (bp) region 3 to the previously identified fatty acid response element was identified as critical for the induction of OLE1 in response to these stimuli using OLE1 promoter-lacZ reporter constructs. Electromobility shift assays confirmed the presence of an inducible band shift in response to hypoxia and cobalt. Mutational analysis defined the nonameric sequence ACTCAACAA as necessary for transactivation. A 20-base pair oligonucleotide containing this nonamer confers up-regulation by hypoxia and inhibition by unsaturated fatty acids when placed upstream of a heterologous promoter in a lacZ reporter construct. Additional yeast genes were identified which respond to hypoxia and cobalt in a manner similar to OLE1. A number of mammalian genes are also up-regulated by hypoxia, cobalt, nickel, and iron chelators. Hence, the identification of a family of yeast genes regulated in a similar manner has implications for understanding oxygen sensing and signaling in eukaryotes.

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Section: Rap1p and Lore-binding Protein(s) (Lbp)-mentioning

confidence: 99%

“…One of these genes, the anaerobically-induced gene, TIR1, encodes a stress-induced cell wall mannoprotein, and is also a member of the seripauperine (PAU) family (35,37,53). The in vivo function of a putative LORE in its promoter region (Ϫ344 to Ϫ325) is not known.…”

Section: Rap1p and Lore-binding Protein(s) (Lbp)-mentioning

confidence: 99%

Identification and Characterization of a Low Oxygen Response Element Involved in the Hypoxic Induction of a Family ofSaccharomyces cerevisiae Genes

Vasconcelles

Jiang

McDaid

et al. 2001

Journal of Biological Chemistry

106

126

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“…All the sequences except peak 5 were identical to sequences within the protein encoded by TIRIISRPI (Fig. 4), which has previously been identified as a gene induced by glucose [35], cold shock [25] or anaerobiosis [36]. Tirlp/Srplp has no consensus sequence for N-linked sugar binding.…”

Section: Resultsmentioning

confidence: 75%

“…It has been hypothesized that these proteins are synthesized as glycosylPtdIns-anchored proteins, secreted to the cell membrane and transferred to a-1,6-glucan which is bound to P-1,3-glucan of the cell wall. Since TirlpISrplp is considered to be a glycosylPtdIns-anchored protein [36], it could be secreted and anchored to the cell wall glucan in the same way.…”

Section: Discussionmentioning

confidence: 99%

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Identification and Analysis of a Static Culture‐Specific Cell Wall Protein, Tir1p/Srp1p in Saccharomyces Cerevisiae

Kitagaki

Shimoi

Itoh

1997

European Journal of Biochemistry

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A 100-kDa protein was found to be a major cell wall protein in Saccharomyces cereviJiae cells cultured without shaking, but was not present in cells cultured with shaking. The amino acid sequence of this protein was identical to the sequence of Tirlp/Srplp. TlRllSRPl has previously been identified as a gene induced by glucose, cold shock or anaerobiosis and was believed to be a cell membrane protein but not a cell wall protein. However, we found that P-l,3-glucanase solubilized Tirlp/Srplp from the cell wall and the purified Tirlp/Srplp reacted with antiserum to P-1,6-glucan and contained glucose. These results suggest that Tirlp/Srplp is a major structural cell wall protein in the static-cultured yeast cells and is bound to the cell wall through p-1,6-glucan. TIRIISRPl mRNA was transcribed only in the static culture and its transcription was regulated by the ROXl repressor.Keywords: TlRl ; SRPl ; yeast cell wall protein; anaerobic conditions; Rarobacter faecitabidus protease I.Saccharomyces cerevisiae has a rigid cell wall outside its cell membrane [ l , 21. When observed under the electron microscope, the cell wall appears as a layered structure, exhibiting a fibrillar or brush-like outer layer, very rich in mannoproteins, and a transparent and amorphous inner layer, which is mainly composed of glucan [3]. This cell wall is considered to have several functions. It protects the cells from mechanical injury, hypotonic lysis and damaging extracellular enzymes. It also contains many hydrolytic enzymes to facilitate assimilation of nutrients. Another important function of the cell wall is to attach cells to other cells. This attachment is observed in sexual agglutination [4, 51, flocculation [6] and pathogenic attachment to host cells [7].The composition of the cell wall is mainly P-glucan and mannoproteins [I, 21. Chitin is a minor component and is found mostly in bud scars. P-Glucan is comprised of P-1,3-glucan and /l-1,6-glucan. These two types of p-glucan are synthesized by completely different pathways. Mannoproteins are glycoproteins with 0-linked oligomannoses andor N-linked high-mannosetype oligosaccharides having a highly branched outer chain of mannose. Mannoproteins in the yeast cell wall are grouped into two classes [l]. One class is comprised of proteins that are extracted with SDS. These proteins are considered to be non-covalently entrapped in the cell wall. The other class is proteins that are not extracted with SDS [8-lo]. These proteins contain structural cell wall proteins and are covalently bound to the cell wall glucan. They can be solubilized by incubation with /l-1,3-glucanase, which digests the insoluble glucan network [ l l ] or with yeast-lytic protease, which digests mannoproteins [ 121.Because of difficulties in purification and characterization of structural cell wall proteins, only Cwplp, Cwp2p and Tiplp [13, 141 have so far been identified from extracts of the cell walls In previous reports [13, 151, cell wall proteins were prepared from cells grown aerobically with shaking. However...

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In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins ofSaccharomyces cerevisiae

Caro

Tettelin

Vossen

et al. 1997

Yeast

316

325

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Use of the Von Heijne algorithm allowed the identification of 686 open reading frames (ORFs) in the genome of Saccharomyces cerevisiae that encode proteins with a potential N-terminal signal sequence for entering the secretory pathway. On further analysis, 51 of these proteins contain a potential glycosyl-phosphatidylinositol (GPI)attachment signal. Seven additional ORFs were found to belong to this group. Upon examination of the possible GPI-attachment sites, it was found that in yeast the most probable amino acids for GPI-attachment are asparagine and glycine.In yeast, GPI-proteins are found at the cell surface, either attached to the plasma-membrane or as an intrinsic part of the cell wall. It was noted that plasma-membrane GPI-proteins possess a dibasic residue motif just before their predicted GPI-attachment site. Based on this, and on homologies between proteins, families of plasma-membrane and cell wall proteins were assigned, revealing 20 potential plasma-membrane and 38 potential cell wall proteins. For members of three plasma-membrane protein families, a function has been described. On the other hand, most of the cell wall proteins seem to be structural components of the wall, responsive to different growth conditions.The GPI-attachment site of yeast slightly differs from mammalian cells. This might be of use in the development of anti-fungal drugs. 1997 John Wiley & Sons, Ltd.

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Regulation by low temperatures and anaerobiosis of a yeast gene specifying a putative GPI‐anchored plasma membrane

Cited by 56 publications

References 44 publications

Identification and Characterization of a Low Oxygen Response Element Involved in the Hypoxic Induction of a Family ofSaccharomyces cerevisiae Genes

Identification and Characterization of a Low Oxygen Response Element Involved in the Hypoxic Induction of a Family ofSaccharomyces cerevisiae Genes

Identification and Analysis of a Static Culture‐Specific Cell Wall Protein, Tir1p/Srp1p in Saccharomyces Cerevisiae

In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins ofSaccharomyces cerevisiae

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