High impact information on TIR1

• NSR1 has three regions: an acidic/serine-rich NH2 terminus, two RNA recognition motifs, and a glycine/arginine-rich COOH terminus [1].
• Intensive deletion analysis has further defined a specific acidic/serine-rich region within the NH2 terminus as necessary for nucleolar accumulation rather than nucleolar targeting [1].
• This serine-rich, multiply-phosphorylated sequence consists of at least three interdependent subdomains required for transcriptional activation [2].
• CDC68 encodes a 1,035-amino-acid protein with a highly acidic and serine-rich carboxyl terminus [3].
• We have determined the nucleotide sequence of the gene and found that it encodes a lysine-rich, serine-rich protein of 152 kilodaltons [4].

Biological context of TIR1

• Hypoxic SRP1/TIR1 gene expression depends on the absence of haem but is independent of Rox1-mediated repression [5].
• Yeast gene SRP1 (serine-rich protein). Intragenic repeat structure and identification of a family of SRP1-related DNA sequences [6].
• In the present study, we show that the SR-like proteins Srp1 and Srp2, found in the fission yeast Schizosaccharomyces pombe, interact with each other and the interaction is modulated by protein phosphorylation [7].
• Seripauperins of Saccharomyces cerevisiae: a new multigene family encoding serine-poor relatives of serine-rich proteins [8].
• The amino acid sequence of this protein was identical to the sequence of Tir1p/Srp1p [9].

Anatomical context of TIR1

• The hypoxic SRP1/TIR1 gene encodes a stress-response cell wall mannoprotein and this gene is downregulated at acidic pH [10].

Associations of TIR1 with chemical compounds

• The hypoxic SRP1/TIR1 gene encodes a stress-response cell wall mannoprotein, which is shown to be necessary for yeast growth at acidic pH in the presence of sodium dodecyl sulfate [11].
• The cDNA sequence encoding Nopp52 predicts a polypeptide whose amino-terminal half consists of multiple acidic/serine-rich regions alternating with basic/proline-rich regions [12].
• An amino-terminal domain containing a signal sequence and a carboxy-terminal domain with homology to GPI (glycosyl-phosphatidyl-inositol) anchor-containing proteins are separated by a central domain containing a highly repeated threonine- and serine-rich sequence [13].
• However, both plant SR proteins are rich in proline, and SR45, unlike most animal SR proteins, has two distinct arginine/serine-rich domains separated by an RNA recognition motif [14].
• In addition to the RING-H2 motif, the predicted protein has a C4 zinc finger, an acidic region, a glycine-rich cluster, and a serine-rich cluster [15].

Other interactions of TIR1

• Thus, cAMP allows partial relief of the TIR1 repression exerted by Ord1p [10].
• However, unlike known HOG pathway-dependent genes, TIR1 is under positive cAMP control and this effect is mediated by GPA2 but not by RAS2 [10].
• The predicted protein sequence of TIR2 demonstrates remarkable homology to TIR1 (72.2%) and is also homologous with TIP1 (49%) [16].
• Disruptions of TIR1, TIR3, or TIR4 prevent anaerobic growth, indicating that each protein is essential for anaerobic adaptation [17].
• We found that a pmt1 deletion mutant was highly sensitive to zymolyase and that in this strain the alpha-galactosidase-Srp1 fusion proteins, an alpha-galactosidase-Sed1 hybrid protein and an alpha-galactosidase-alpha-agglutinin hybrid protein were absent from both the membrane and the cell wall fractions [18].

References