Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
52
|
pubmed:dateCreated |
1999-2-3
|
pubmed:abstractText |
The levels of mRNA and protein encoded by the c-myc protooncogene set the balance between proliferation and differentiation of mammalian cells. Thus, it is essential for the cell to tightly control c-myc expression. Indeed, cells utilize many mechanisms to control c-myc expression, including transcription, RNA processing, translation, and protein stability. We have focused on turnover of c-myc mRNA as a key modulator of the timing and level of c-myc expression. c-myc mRNA is labile in cells, and its half-life is controlled by multiple instability elements located within both the coding region and the 3'-untranslated region (3'-UTR). Much work has focused on the protein factors that bind the instability elements, yet little is known about the enzymatic activities that effect the degradation of c-myc mRNA. Here I have utilized a novel cell-free mRNA decay system to characterize the c-myc mRNA decay machinery. This machinery consists of 3' to 5' mRNA decay activities that are Mg2+-dependent, require neither exogenous ATP/GTP nor an ATP-regenerating system, and act independently of a 7mG(5')ppp(5')G cap structure to deadenylate an exogenous mRNA substrate in a c-myc 3'-UTR-dependent fashion. Following deadenylation, nucleolytic decay of the 3'-UTR occurs generating 3' decay intermediates via a ribonucleolytic activity that can assemble on the c-myc 3'-UTR in a poly(A)-independent manner.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3' Untranslated Regions,
http://linkedlifedata.com/resource/pubmed/chemical/Globins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
273
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
34770-4
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:9857001-3' Untranslated Regions,
pubmed-meshheading:9857001-Cell-Free System,
pubmed-meshheading:9857001-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:9857001-Globins,
pubmed-meshheading:9857001-Half-Life,
pubmed-meshheading:9857001-Humans,
pubmed-meshheading:9857001-Polyribosomes,
pubmed-meshheading:9857001-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:9857001-RNA, Messenger,
pubmed-meshheading:9857001-RNA, Neoplasm,
pubmed-meshheading:9857001-Recombinant Fusion Proteins
|
pubmed:year |
1998
|
pubmed:articleTitle |
Characterization of c-myc 3' to 5' mRNA decay activities in an in vitro system.
|
pubmed:affiliation |
Department of Microbiology and Immunology, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157-1064, USA. gbrewer@wfubmc.edu
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|