Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6 Pt 1
pubmed:dateCreated
1991-3-1
pubmed:abstractText
Two strains of Saccharomyces cerevisiae were constructed that are conditional for synthesis of the 60S ribosomal subunit protein, L16, or the 40S ribosomal subunit protein, rp59. These strains were used to determine the effects of depriving cells of either of these ribosomal proteins on ribosome assembly and on the synthesis and stability of other ribosomal proteins and ribosomal RNAs. Termination of synthesis of either protein leads to diminished accumulation of the subunit into which it normally assembles. Depletion of L16 or rp59 has no effect on synthesis of most other ribosomal proteins or ribosomal RNAs. However, most ribosomal proteins and ribosomal RNAs that are components of the same subunit as L16 or rp59 are rapidly degraded upon depletion of L16 or rp59, presumably resulting from abortive assembly of the subunit. Depletion of L16 has no effect on the stability of most components of the 40S subunit. Conversely, termination of synthesis of rp59 has no effect on the stability of most 60S subunit components. The implications of these findings for control of ribosome assembly and the order of assembly of ribosomal proteins into the ribosome are discussed.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-17248617, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-2183018, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-2406561, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-2476649, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-2540422, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-2642897, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-2658053, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-2666845, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-2839305, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-284338, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-3047007, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-3275866, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-3279045, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-3282992, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-3308884, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-3329033, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-340929, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-353511, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-3537704, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-3537715, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-377016, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-377017, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-3897837, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-393511, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-4557192, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-4579428, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-4617153, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-4868216, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-4912319, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-4922290, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-510305, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-5540996, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-592369, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-6083441, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-6092912, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-6206783, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-6310324, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-6765595, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-7012374, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-7050661, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-7105180, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-772413, http://linkedlifedata.com/resource/pubmed/commentcorrection/2277060-775493
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:volume
111
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2261-74
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Depletion of yeast ribosomal proteins L16 or rp59 disrupts ribosome assembly.
pubmed:affiliation
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.