Linked Life Data

7608167

Source:http://linkedlifedata.com/resource/pubmed/id/7608167

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1995-8-16
pubmed:abstractText
5'-Exonuclease-2 has been purified 17,000-fold from whole cell extracts of Saccharomyces cerevisiae. A 116-kDa polypeptide parallels the enzyme activity when the purified protein is examined by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Amino-terminal sequencing of the 116-kDa protein shows that the sequence agrees with that encoded by the HKE1 gene, previously reported to encode exonuclease-2. A 45-kDa polypeptide also parallels the enzyme activity upon purification, and Sephacryl S-200 molecular sieve chromatography of the purified enzyme shows a parallel elution of most of the 116- and 45-kDa polypeptides, suggesting a close association of the two. Enzyme instability has precluded a more detailed analysis of their associative properties. The enzyme hydrolyzes RNA substrates to 5'-mononucleotides in a processive manner. Measurements of its substrate specificity and mode of action are compared with 5'-exonuclease-1. Restriction cut single-stranded T7 DNA is hydrolyzed at approximately 5-7% of the rate of 18 S rRNA of yeast by both enzymes. That 5'-exonuclease-2 hydrolyzes in a processive manner and lacks endonuclease activity is shown by the finding that [5'-32P]GMP is the only product of its hydrolysis of [alpha-32P]GTP-labeled synthetic RNAs. That 5'-exonuclease-2 hydrolyzes by a 5'-->3' mode is shown by: 1) its poor hydrolysis of both 5'-capped and triphosphate-ended RNA substrates; 2) the products of its hydrolysis of [5'-32P,3H](pA)4; and 3) the accumulation of 3'-stall fragments when a strong artificial RNA secondary structure is present in synthetic RNAs. 5'-Exonuclease-1 hydrolyzes the synthetic RNAs and (pA)4 in an identical manner.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Exoribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/KEM1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Phosphodiesterase I, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Poly A, http://linkedlifedata.com/resource/pubmed/chemical/RAT1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
270
pubmed:geneSymbol
HKE1, XRN1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16063-9
pubmed:dateRevised
2009-5-28
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
5'-exonuclease-2 of Saccharomyces cerevisiae. Purification and features of ribonuclease activity with comparison to 5'-exonuclease-1.
pubmed:affiliation
Biology Division, Oak Ridge National Laboratory, Tennessee 37831-8080, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't