Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1990 Jun;110(6):1897-909.
doi: 10.1083/jcb.110.6.1897.

Sec2 protein contains a coiled-coil domain essential for vesicular transport and a dispensable carboxy terminal domain

J Nair  1 , H Müller, M Peterson, P Novick
Affiliations

Sec2 protein contains a coiled-coil domain essential for vesicular transport and a dispensable carboxy terminal domain

J Nair et al. J Cell Biol. 1990 Jun.

Abstract

SEC2 function is required at the post-Golgi apparatus stage of the yeast secretory pathway. The SEC2 sequence encodes a protein product of 759 amino acids containing an amino terminal region that is predicted to be in an alpha-helical, coiled-coil conformation. Two temperature-sensitive alleles, sec2-41 and sec2-59, encode proteins truncated by opal stop codons and are suppressible by an opal tRNA suppressor. Deletion analysis indicates that removal of the carboxyl terminal 251 amino acids has no apparent phenotype, while truncation of 368 amino acids causes temperature sensitivity. The amino terminal half of the protein, containing the putative coiled-coil domain, is essential at all temperatures. Sec2 protein is found predominantly in the soluble fraction and displays a native molecular mass of greater than 500 kD. All phenotypes of the temperature-sensitive sec2 alleles are partially suppressed by duplication of the SEC4 gene, but the lethality of a sec2 disruption is not suppressed. The sec2-41 mutation exhibits synthetic lethality with the same subset of the late acting sec mutants as does sec4-8 and sec15-1. The Sec2 protein may function in conjunction with the Sec4 and Sec15 proteins to control vesicular traffic.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Mol Gen Genet. 1985;201(1):82-7 - PubMed
    1. Cell. 1988 Jun 3;53(5):669-71 - PubMed
    1. Science. 1985 Mar 22;227(4693):1435-41 - PubMed
    1. J Biol Chem. 1985 Feb 10;260(3):1513-20 - PubMed
    1. Proc Natl Acad Sci U S A. 1987 Dec;84(24):8898-902 - PubMed

Publication types

Associated data