| pubmed-article:7608167 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7608167 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
| pubmed-article:7608167 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:7608167 | lifeskim:mentions | umls-concept:C1148840 | lld:lifeskim |
| pubmed-article:7608167 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:7608167 | lifeskim:mentions | umls-concept:C2348519 | lld:lifeskim |
| pubmed-article:7608167 | pubmed:issue | 27 | lld:pubmed |
| pubmed-article:7608167 | pubmed:dateCreated | 1995-8-16 | lld:pubmed |
| pubmed-article:7608167 | 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. | lld:pubmed |
| pubmed-article:7608167 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7608167 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7608167 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7608167 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7608167 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7608167 | pubmed:author | pubmed-author:StevensAA | lld:pubmed |
| pubmed-article:7608167 | pubmed:author | pubmed-author:PooleT LTL | lld:pubmed |
| pubmed-article:7608167 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7608167 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:7608167 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7608167 | pubmed:geneSymbol | XRN1 | lld:pubmed |
| pubmed-article:7608167 | pubmed:geneSymbol | HKE1 | lld:pubmed |
| pubmed-article:7608167 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7608167 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7608167 | pubmed:pagination | 16063-9 | lld:pubmed |
| pubmed-article:7608167 | pubmed:dateRevised | 2009-5-28 | lld:pubmed |
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| pubmed-article:7608167 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7608167 | pubmed:articleTitle | 5'-exonuclease-2 of Saccharomyces cerevisiae. Purification and features of ribonuclease activity with comparison to 5'-exonuclease-1. | lld:pubmed |
| pubmed-article:7608167 | pubmed:affiliation | Biology Division, Oak Ridge National Laboratory, Tennessee 37831-8080, USA. | lld:pubmed |
| pubmed-article:7608167 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7608167 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7608167 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:7608167 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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