A novel autonomously replicating sequence (ARS) for multiple integration in the yeast Hansenula polymorpha DL-1

Sohn, Jae Hak; Choi, Eui Sung; Kim, Chul Ho; Agaphonov, Michael O.; Ter‐Avanesyan, Michael D.; Rhee, Jae-Sung; Rhee, Shin Hyung

doi:10.1128/jb.178.15.4420-4428.1996

Cited by 70 publications

(76 citation statements)

References 39 publications

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“…Several H. polymorpha autonomously replicating sequences (HARS) and other DNA-fragments that promote autonomous replication of plasmids in H. polymorpha have been isolated and are currently being used in various vectors [8,[13][14][15][16][17][18]. The DNA fragment that contains the S. cerevisiae LEU2 gene as the selectable marker has also been shown to promote autonomous replication in H. polymorpha [18].…”

Section: Expression Vectorsmentioning

confidence: 99%

The methylotrophic yeast Hansenula polymorpha: a versatile cell factory

Dijk

Faber

Kiel

et al. 2000

Enzyme and Microbial Technology

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Section: Expression Vectorsmentioning

confidence: 99%

The methylotrophic yeast Hansenula polymorpha: a versatile cell factory

Dijk

Faber

Kiel

et al. 2000

Enzyme and Microbial Technology

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“…All RSTs were, nevertheless, compared to the complete sequence of the S. cerevisiae 2-micron plasmid but no similarity was found. In addition, no RST was similar to the autonomously replicating sequence HARS36 of the P. angusta DL-1 strain [20].…”

Section: Plasmids and Autonomously Replicating Sequencesmentioning

confidence: 94%

Genomic Exploration of the Hemiascomycetous Yeasts: 13. Pichia angusta

et al. 2000

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As part of a comparative genomics project on 13 hemiascomycetous yeasts, the Pichia angusta type strain was studied using a partial random sequencing strategy. With coverage of 0.5 genome equivalents, about 2500 novel proteincoding genes were identified, probably corresponding to more than half of the P. angusta protein-coding genes, 6% of which do not have homologs in Saccharomyces cerevisiae. Some of them contain one or two introns, on average three times shorter than those in S. cerevisiae. We also identified 28 tRNA genes, a few retrotransposons similar to Ty5 of S. cerevisiae, solo long terminal repeats, the whole ribosomal DNA cluster, and segments of mitochondrial DNA. The P. angusta sequences were deposited in EMBL under the accession numbers AL430961 to AL436044. ß 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

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“…To construct the pMCOP1-L plasmid, the 5Ј part of the HpRET1 gene (the 882-bp EspI-BglII fragment of the p27OPU8 plasmid) was fused with the MOX promoter (the 0.9-kb StuI-ScaI fragment of pMMU [5]) and inserted together with the ScLEU2 selectable marker (the 1.6-kb BsrGI-SacI fragment of pJJ282) into the StuI-SacI sites of the pUK21 plasmid (49). The pH5 plasmid was constructed by insertion of the 1.3-kb NotI-EcoRV fragment of pCHLX (45) into the NotI and SmaI sites of the pE1 plasmid (29).…”

Section: Methodsmentioning

confidence: 99%

C-Terminal Truncation of α-COP Affects Functioning of Secretory Organelles and Calcium Homeostasis in Hansenula polymorpha

et al. 2004

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In eukaryotic cells, COPI vesicles retrieve resident proteins to the endoplasmic reticulum and mediate intra-Golgi transport. Here, we studied the Hansenula polymorpha homologue of the Saccharomyces cerevisiae RET1 gene, encoding ␣-COP, a subunit of the COPI protein complex. H. polymorpha ret1 mutants, which expressed truncated ␣-COP lacking more than 300 C-terminal amino acids, manifested an enhanced ability to secrete human urokinase-type plasminogen activator (uPA) and an inability to grow with a shortage of Ca 2؉ ions, whereas a lack of ␣-COP expression was lethal. The ␣-COP defect also caused alteration of intracellular transport of the glycosylphosphatidylinositol-anchored protein Gas1p, secretion of abnormal uPA forms, and reductions in the levels of Pmr1p, a Golgi Ca 2؉ -ATPase. Overexpression of Pmr1p suppressed some ret1 mutant phenotypes, namely, Ca 2؉ dependence and enhanced uPA secretion. The role of COPI-dependent vesicular transport in cellular Ca 2؉ homeostasis is discussed.In eukaryotic cells, secretory proteins synthesized at the endoplasmic reticulum (ER) pass through multiple distinct membrane-bound organelles comprising the secretory pathway. Transport of proteins and lipids between membrane compartments of the early secretory system is mediated by COPIand COPII-coated vesicles that capture cargo, bud from the donor membrane, and then target, dock, and fuse with an appropriate acceptor compartment (40). Both the COPI and COPII protein coat complexes employ a GTP switch mechanism for coating and uncoating. The COPII complex mediates selective protein export from the ER, while COPI-coated vesicles retrieve resident proteins to the ER and mediate intraGolgi transport (8,38).The Golgi apparatus is composed of distinct cisternal regions, namely, the cis, medial, trans-Golgi, and trans-Golginetwork regions (13). Secretory cargo proteins passing through the Golgi apparatus are modified by the unique sets of resident enzymes of different subcompartments. Two alternative models for the origin of the Golgi subcompartments suggest different roles for COPI vesicles in secretory cargo transport and the function of the Golgi apparatus. In the stable-compartments model, anterograde COPI vesicles carry secretory cargo forward and exclude resident Golgi proteins. In the cisternalmaturation model, entire cisternae carry secretory cargo forward, and retrograde COPI vesicles recycle resident Golgi proteins to younger cisternae. Thus, the distinction between the two models centers on the contents of COPI vesicles and the directionality of their transport. However, recent experimental data indicate that intra-Golgi COPI traffic has a bidirectional character (for reviews, see references 23 and 38). Moreover, the dynamics of cisternal progression and vesicular traffic are different in higher eukaryotes versus yeasts. Progression of the tightly stacked Golgi cisternae of animal cells occurs at a significantly lower rate than the traffic of most cargoes through the secretory pathway. COPI vesicles mediating cargo tra...

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A novel autonomously replicating sequence (ARS) for multiple integration in the yeast Hansenula polymorpha DL-1

Cited by 70 publications

References 39 publications

The methylotrophic yeast Hansenula polymorpha: a versatile cell factory

The methylotrophic yeast Hansenula polymorpha: a versatile cell factory

Genomic Exploration of the Hemiascomycetous Yeasts: 13. Pichia angusta

C-Terminal Truncation of α-COP Affects Functioning of Secretory Organelles and Calcium Homeostasis in Hansenula polymorpha

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