« Previous AbstractAllocating nitrogen away from a herbivore: a novel compensatory response to root herbivory    Next AbstractComposition of Unrecorded Distilled Alcohol (bai jiu) Produced in Small Rural Factories in Central China »

J Cell Biol

Title:		Characterization of new mutants in the early part of the yeast secretory pathway isolated by a [3H]mannose suicide selection
Author(s):		Newman AP; Ferro-Novick S;
Address:		"Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510"
Journal Title:		J Cell Biol
Year:		1987
Volume:		105
Issue:		4
Page Number:		1587 - 1594
DOI:		10.1083/jcb.105.4.1587
ISSN/ISBN:		0021-9525 (Print) 1540-8140 (Electronic) 0021-9525 (Linking)
Abstract:		"We have adapted a [3H]mannose suicide selection to identify mutations in additional genes which function in the early part of the yeast secretory pathway. Thus far this protocol has led to the identification of two new genes which are implicated in this process, as well as additional alleles of previously identified genes. The new mutants, bet1 and bet2, are temperature sensitive for growth and protein transport. Thin section analysis has revealed the accumulation of a network of endoplasmic reticulum (ER) at the restrictive temperature (37 degrees C). Precursors of exported proteins that accumulate in the cell at 37 degrees C are terminally core glycosylated. These observations suggest that the transport of precursors is blocked subsequent to translocation into the ER but before entry into the Golgi apparatus. The bet1 and bet2 mutants define two new complementation groups which have the same properties as previously identified ER-accumulating mutants. This and previous findings (Novick, P., C. Field, and R. Schekman, 1980, Cell, 21:205-215) suggest that protein exit from the ER and entry into the Golgi apparatus is a complex process requiring at least 11 genes"
Keywords:		"Acid Phosphatase/metabolism Biological Transport Cell Survival Endoplasmic Reticulum/ultrastructure Fungal Proteins/*metabolism Glycoside Hydrolases/metabolism Mannose/metabolism Mating Factor Microscopy, Electron Molecular Weight Mutation Peptides/metabo;"
Notes:		"MedlineNewman, A P Ferro-Novick, S eng GM 35421-02/GM/NIGMS NIH HHS/ RR 05358/RR/NCRR NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1987/10/01 J Cell Biol. 1987 Oct; 105(4):1587-94. doi: 10.1083/jcb.105.4.1587"