PNG1, a Yeast Gene Encoding a Highly Conserved Peptide:N-glycanase

Overview

Journal J Cell Biol

Specialty Cell Biology

Date 2000 Jun 1

PMID 10831608

Citations 86

Authors

T Suzuki

H Park

N M Hollingsworth

R Sternglanz

W J Lennarz

Affiliations

Soon will be listed here.

Abstract

It has been proposed that cytoplasmic peptide:N-glycanase (PNGase) may be involved in the proteasome-dependent quality control machinery used to degrade newly synthesized glycoproteins that do not correctly fold in the ER. However, a lack of information about the structure of the enzyme has limited our ability to obtain insight into its precise biological function. A PNGase-defective mutant (png1-1) was identified by screening a collection of mutagenized strains for the absence of PNGase activity in cell extracts. The PNG1 gene was mapped to the left arm of chromosome XVI by genetic approaches and its open reading frame was identified. PNG1 encodes a soluble protein that, when expressed in Escherichia coli, exhibited PNGase activity. PNG1 may be required for efficient proteasome-mediated degradation of a misfolded glycoprotein. Subcellular localization studies indicate that Png1p is present in the nucleus as well as the cytosol. Sequencing of expressed sequence tag clones revealed that Png1p is highly conserved in a wide variety of eukaryotes including mammals, suggesting that the enzyme has an important function.

Citing Articles

Development of new NGLY1 assay systems - toward developing an early screening method for NGLY1 deficiency.

Hirayama H, Fujihira H, Suzuki T Glycobiology. 2024; 34(11).

PMID: 39206713 PMC: 11442003. DOI: 10.1093/glycob/cwae067.

Bi-directionalized promoter systems allow methanol-free production of hard-to-express peroxygenases with Komagataella Phaffii.

Besleaga M, Zimmermann C, Ebner K, Mach R, Mach-Aigner A, Geier M Microb Cell Fact. 2024; 23(1):177.

PMID: 38879507 PMC: 11179361. DOI: 10.1186/s12934-024-02451-9.

Intranasal oxytocin suppresses seizure-like behaviors in a mouse model of NGLY1 deficiency.

Makita Y, Asahina M, Fujinawa R, Yukitake H, Suzuki T Commun Biol. 2024; 7(1):460.

PMID: 38649481 PMC: 11035592. DOI: 10.1038/s42003-024-06131-7.

The Impact of Glycoengineering on the Endoplasmic Reticulum Quality Control System in Yeasts.

Piirainen M, Frey A Front Mol Biosci. 2022; 9:910709.

PMID: 35720120 PMC: 9201249. DOI: 10.3389/fmolb.2022.910709.

Comprehensive Analysis of the Structure and Function of Peptide:N-Glycanase 1 and Relationship with Congenital Disorder of Deglycosylation.

Miao X, Wu J, Chen H, Lu G Nutrients. 2022; 14(9).

PMID: 35565658 PMC: 9102325. DOI: 10.3390/nu14091690.

References

Plemper R, Wolf D . Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem Sci. 1999; 24(7):266-70. DOI: 10.1016/s0968-0004(99)01420-6. View

Weng S, Spiro R . Demonstration of a peptide:N-glycosidase in the endoplasmic reticulum of rat liver. Biochem J. 1997; 322 ( Pt 2):655-61. PMC: 1218239. DOI: 10.1042/bj3220655. View

Hill J, Myers A, Koerner T, Tzagoloff A . Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast. 1986; 2(3):163-7. DOI: 10.1002/yea.320020304. View

Yu H, Kaung G, Kobayashi S, Kopito R . Cytosolic degradation of T-cell receptor alpha chains by the proteasome. J Biol Chem. 1997; 272(33):20800-4. DOI: 10.1074/jbc.272.33.20800. View

Romisch K . Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane. J Cell Sci. 1999; 112 ( Pt 23):4185-91. DOI: 10.1242/jcs.112.23.4185. View

Berger S, Menudier A, Julien R, Karamanos Y . Do de-N-glycosylation enzymes have an important role in plant cells?. Biochimie. 1995; 77(9):751-60. DOI: 10.1016/0300-9084(96)88193-4. View

Glas R, Bogyo M, McMaster J, Gaczynska M, Ploegh H . A proteolytic system that compensates for loss of proteasome function. Nature. 1998; 392(6676):618-22. DOI: 10.1038/33443. View

Halaban R, Cheng E, Zhang Y, Moellmann G, Hanlon D, Michalak M . Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc Natl Acad Sci U S A. 1997; 94(12):6210-5. PMC: 21028. DOI: 10.1073/pnas.94.12.6210. View

Sikorski R, Hieter P . A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 1989; 122(1):19-27. PMC: 1203683. DOI: 10.1093/genetics/122.1.19. View

10.

Osmulski P, Gaczynska M . A new large proteolytic complex distinct from the proteasome is present in the cytosol of fission yeast. Curr Biol. 1998; 8(18):1023-6. DOI: 10.1016/s0960-9822(07)00423-x. View

11.

Gillece P, Luz J, Lennarz W, de la Cruz F, Romisch K . Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J Cell Biol. 1999; 147(7):1443-56. PMC: 2174254. DOI: 10.1083/jcb.147.7.1443. View

12.

Suzuki T, Lennarz W . In yeast the export of small glycopeptides from the endoplasmic reticulum into the cytosol is not affected by the structure of their oligosaccharide chains. Glycobiology. 1999; 10(1):51-8. DOI: 10.1093/glycob/10.1.51. View

13.

Horton R, Cai Z, Ho S, Pease L . Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction. Biotechniques. 1990; 8(5):528-35. View

14.

Kitajima K, Suzuki T, Kouchi Z, Inoue S, Inoue Y . Identification and distribution of peptide:N-glycanase (PNGase) in mouse organs. Arch Biochem Biophys. 1995; 319(2):393-401. DOI: 10.1006/abbi.1995.1309. View

15.

Suzuki T, Kitajima K, Emori Y, Inoue Y, Inoue S . Site-specific de-N-glycosylation of diglycosylated ovalbumin in hen oviduct by endogenous peptide: N-glycanase as a quality control system for newly synthesized proteins. Proc Natl Acad Sci U S A. 1997; 94(12):6244-9. PMC: 21034. DOI: 10.1073/pnas.94.12.6244. View

16.

Huppa J, Ploegh H . The alpha chain of the T cell antigen receptor is degraded in the cytosol. Immunity. 1997; 7(1):113-22. DOI: 10.1016/s1074-7613(00)80514-2. View

17.

Longtine M, McKenzie 3rd A, DeMarini D, Shah N, Wach A, Brachat A . Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast. 1998; 14(10):953-61. DOI: 10.1002/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U. View

18.

Geier E, Pfeifer G, Wilm M, Baumeister W, Eichmann K, Niedermann G . A giant protease with potential to substitute for some functions of the proteasome. Science. 1999; 283(5404):978-81. DOI: 10.1126/science.283.5404.978. View

19.

Graham T, Scott P, Emr S . Brefeldin A reversibly blocks early but not late protein transport steps in the yeast secretory pathway. EMBO J. 1993; 12(3):869-77. PMC: 413285. DOI: 10.1002/j.1460-2075.1993.tb05727.x. View

20.

Suzuki T, Kitajima K, Inoue S, Inoue Y . Occurrence and biological roles of 'proximal glycanases' in animal cells. Glycobiology. 1994; 4(6):777-89. DOI: 10.1093/glycob/4.6.777. View