Cargando…
Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry
The structure of rat liver vault ribonucleoprotein particles was examined using several different staining techniques in conjunction with EM and digestion with hydrolytic enzymes. Quantitative scanning transmission EM demonstrates that each vault particle has a total mass of 12.9 +/- 1 MD and contai...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1991
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2288824/ https://www.ncbi.nlm.nih.gov/pubmed/1988458 |
_version_ | 1782152116022804480 |
---|---|
collection | PubMed |
description | The structure of rat liver vault ribonucleoprotein particles was examined using several different staining techniques in conjunction with EM and digestion with hydrolytic enzymes. Quantitative scanning transmission EM demonstrates that each vault particle has a total mass of 12.9 +/- 1 MD and contains two centers of mass, suggesting that each vault particle is a dimer. Freeze-etch reveals that each vault opens into delicate flower-like structures, in which eight rectangular petals are joined to a central ring, each by a thin hook. Vaults examined by negative stain and conventional transmission EM (CTEM) also reveal the flower-like structure. Trypsin treatment of vaults resulted exclusively in cleavage of the major vault protein (p104) and concurrently alters their structure as revealed by negative stain/CTEM, consistent with a localization of p104 to the flower petals. We propose a structural model that predicts the stoichiometry of vault proteins and RNA, defines vault dimer-monomer interactions, and describes two possible modes for unfolding of vaults into flowers. These highly dynamic structural variations are likely to play a role in vault function. |
format | Text |
id | pubmed-2288824 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1991 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22888242008-05-01 Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry J Cell Biol Articles The structure of rat liver vault ribonucleoprotein particles was examined using several different staining techniques in conjunction with EM and digestion with hydrolytic enzymes. Quantitative scanning transmission EM demonstrates that each vault particle has a total mass of 12.9 +/- 1 MD and contains two centers of mass, suggesting that each vault particle is a dimer. Freeze-etch reveals that each vault opens into delicate flower-like structures, in which eight rectangular petals are joined to a central ring, each by a thin hook. Vaults examined by negative stain and conventional transmission EM (CTEM) also reveal the flower-like structure. Trypsin treatment of vaults resulted exclusively in cleavage of the major vault protein (p104) and concurrently alters their structure as revealed by negative stain/CTEM, consistent with a localization of p104 to the flower petals. We propose a structural model that predicts the stoichiometry of vault proteins and RNA, defines vault dimer-monomer interactions, and describes two possible modes for unfolding of vaults into flowers. These highly dynamic structural variations are likely to play a role in vault function. The Rockefeller University Press 1991-01-02 /pmc/articles/PMC2288824/ /pubmed/1988458 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry |
title | Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry |
title_full | Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry |
title_fullStr | Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry |
title_full_unstemmed | Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry |
title_short | Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry |
title_sort | vaults. iii. vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2288824/ https://www.ncbi.nlm.nih.gov/pubmed/1988458 |