Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-3-18
pubmed:databankReference
pubmed:abstractText
Ribonucleotide reductase activity is required for generating deoxyribonucleotides for DNA replication. Schizosaccharomyces pombe cells lacking ribonucleotide reductase activity arrest during S phase of the cell cycle. In a screen for hydroxyurea-sensitive mutants in S. pombe, we have identified a gene, liz1(+), which when mutated reveals an additional, previously undescribed role for ribonucleotide reductase activity during mitosis. Inactivation of ribonucleotide reductase, by either hydroxyurea or a cdc22-M45 mutation, causes liz1(-) cells in G2 to undergo an aberrant mitosis, resulting in chromosome missegregation and late mitotic arrest. liz1(+) encodes a 514-amino acid protein with strong similarity to a family of transmembrane transporters, and localizes to the plasma membrane of the cell. These results reveal an unexpected G2/M function of ribonucleotide reductase and establish that defects in a transmembrane protein can affect cell cycle progression.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-1412696, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-1427071, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-1587485, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-2074269, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-2358444, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-2406029, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-2665944, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-2679804, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-2683079, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-3032459, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-3275614, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-3294799, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-3955656, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-7723827, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8019001, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8036497, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8121488, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8141795, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8313905, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8422997, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8479429, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8497322, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8672817, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8939675, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8939848, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8978030, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-8986778, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-9094438, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-9135148, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-9180692, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-9348664, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-9356477, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-9399795, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-9450932, http://linkedlifedata.com/resource/pubmed/commentcorrection/9950674-958201
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1059-1524
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
245-57
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Liz1p, a novel fission yeast membrane protein, is required for normal cell division when ribonucleotide reductase is inhibited.
pubmed:affiliation
Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.