✦ LIBER ✦

Isolation of Pichia pastoris genes involved in ER-to-Golgi transport

✍ Scribed by William E. Payne; Chris A. Kaiser; Brooke J. Bevis; Jon Soderholm; Dragony Fu; Irina B. Sears; Benjamin S. Glick

Publisher: John Wiley and Sons
Year: 2000
Tongue: English
Weight: 359 KB
Volume: 16
Category: Article
ISSN: 0749-503X
DOI: 10.1002/1097-0061(200008)16:11<979::aid-yea594>3.0.co;2-c

No coin nor oath required. For personal study only.

✦ Synopsis

Pichia pastoris has discrete transitional ER sites and coherent Golgi stacks, making this yeast an ideal system for studying the organization of the early secretory pathway. To provide molecular tools for this endeavour, we isolated P. pastoris homologues of the SEC12, SEC13, SEC17, SEC18 and SAR1 genes. The P. pastoris SEC12, SEC13, SEC17 and SEC18 genes were shown to complement the corresponding S. cerevisiae mutants. The SEC17 and SAR1 genes contain introns at the same relative positions in both P. pastoris and S. cerevisiae, whereas the SEC13 gene contains an intron in P. pastoris but not in S. cerevisiae. Intron structure is similar in the two yeasts, although the favoured 5k splice sequence appears to be GTAAGT in P. pastoris vs. GTATGT in S. cerevisiae. The predicted amino acid sequences of Sec13p, Sec17p, Sec18p and Sar1p show strong conservation in the two yeasts. By contrast, the predicted lumenal domain of Sec12p is much larger in P. pastoris, suggesting that this domain may help localize Sec12p to transitional ER sites. A comparison of the SEC12 loci in various budding yeasts indicates that the SEC12-related gene SED4 is probably unique to the Saccharomyces lineage.

📜 SIMILAR VOLUMES

Isolation of Three Contiguous Genes,ACR1

Isolation of Three Contiguous Genes,ACR1,ACR2 andACR3, Involved in Resistance to Arsenic Compounds in the YeastSaccharomyces cerevisiae

✍ Bobrowicz, Piotr; Wysocki, Robert; Owsianik, Grzegorz; Goffeau, André; Ułaszewsk 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 148 KB

A 4.2 kb region from Saccharomyces cerevisiae chromosome XVI was isolated as a yeast fragment conferring resistance to 7 mM-sodium arsenite (NaAsO2), when put on a multicopy plasmid. Homology searches revealed a cluster of three new open reading frames named ACR1, ACR2 and ACR3. The hypothetical pro

Retention of a Duplicate Gene Through Ch

Retention of a Duplicate Gene Through Changes in Subcellular Targeting: An Electron Transport Protein Homologue Localizes to the Golgi

✍ TimothyR. Schmidt; JeffreyW. Doan; Morris Goodman; LawrenceI. Grossman 📂 Article 📅 2003 🏛 Springer 🌐 English ⚖ 210 KB

Expression of genes involved in symbioti

Expression of genes involved in symbiotic carbon and nitrogen transport inPinus taedamycorrhizal roots exposed to CO2enrichment and nitrogen fertilization

✍ Jeri Lynn Parrent; Rytas Vilgalys 📂 Article 📅 2009 🏛 Springer-Verlag 🌐 English ⚖ 350 KB

Nucleotide sequence of the fhuC and fhuD

Nucleotide sequence of the fhuC and fhuD genes involved in iron (III) hydroxamate transport: Domains in FhuC homologous to ATP-binding proteins

✍ Burkhardt, Renate ;Braun, Volkmar 📂 Article 📅 1987 🏛 Springer 🌐 English ⚖ 629 KB

Isolation and characterisation of a muta

Isolation and characterisation of a mutation in the PMR1 gene encoding a Golgi membrane ATPase, which causes hypersensitivity to over-expression of Clb3 in Saccharomyces cerevisiae

✍ Funakoshi, M. ;Kajiwara, R. ;Goda, T. ;Nishimoto, T. ;Kobayashi, H. 📂 Article 📅 2000 🏛 Springer 🌐 English ⚖ 276 KB

Nuclear estrogen receptor II (nER-II) is

Nuclear estrogen receptor II (nER-II) is involved in the estrogen-dependent ribonucleoprotein transport in the goat uterus: II. isolation and characterization of three small nuclear ribonucleoprotein proteins which bind to nER-II

✍ Thomas Sebastian; Raghava Varman Thampan 📂 Article 📅 2002 🏛 John Wiley and Sons 🌐 English ⚖ 212 KB

## Abstract Three proteins of a goat uterine small nuclear ribonucleoprotein (snRNP) fraction, which bind to nuclear estrogen receptor‐II (nER‐II) have been isolated and purified. These are the p32, p55, and p60 of which p32 is the major nER‐II binding protein. Indirect evidence reveals that p32 bi