FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2103245112> ?p ?o ?g. }

• W2103245112 endingPage "36" @default.
• W2103245112 startingPage "27" @default.
• W2103245112 abstract "The terminase enzyme from bacteriophage lambda is a hetero-trimeric complex composed of the viral gpA and gpNu1 proteins (gpA1.gpNu1(2)) and is responsible for packaging a single genome within the viral capsid. Current expression systems for these proteins require thermal induction which may be responsible for the formation of insoluble aggregates observed in E. coli. We report the re-cloning of the terminase subunits into vectors which allow low temperature induction. While this has resulted in increased solubility of the large gpA subunit of the enzyme, the small gpNu1 subunit remains insoluble under all conditions examined. This paper describes the solublization of gpNu1 with guanidinium hydrochloride and purification of the protein to homogeneity. Reconstitution of the enzyme from the individually purified subunits yields a catalytically-competent complex which exhibits activity identical to wild-type enzyme. Thermal denaturation of the proteins was monitored by circular dichroism (CD) spectroscopy and demonstrates that while unfolding of gpA is irreversible, the gpNu1 subunit refolds into a conformation which is essentially identical to the pre-heated protein. Moreover, while denaturation of gpA is highly cooperative, the small subunit unfolds over a wide temperature range and with thermodynamic parameters lower than expected for a small globular protein. Thermally-induced denaturation of the enzyme reconstituted from the individual subunits is highly cooperative with no evidence of multiple transitions. Our data demonstrate that the terminase subunits directly interact in solution, and that this interaction alters the thermal stability of the smaller gpNu1 subunit. The implication of these results with respect to assembly of a catalytically competent enzyme complex are discussed." @default.
• W2103245112 created "2016-06-24" @default.
• W2103245112 creator A5003973944 @default.
• W2103245112 creator A5058346480 @default.
• W2103245112 creator A5071985859 @default.
• W2103245112 creator A5087157615 @default.
• W2103245112 date "1998-07-01" @default.
• W2103245112 modified "2023-09-23" @default.
• W2103245112 title "The phage lambda terminase enzyme: 1. Reconstitution of the holoenzyme from the individual subunits enhances the thermal stability of the small subunit" @default.
• W2103245112 cites W1494276408 @default.
• W2103245112 cites W1496368635 @default.
• W2103245112 cites W1504805812 @default.
• W2103245112 cites W1516304371 @default.
• W2103245112 cites W1527452930 @default.
• W2103245112 cites W1552366385 @default.
• W2103245112 cites W1557773400 @default.
• W2103245112 cites W1565035996 @default.
• W2103245112 cites W1709580310 @default.
• W2103245112 cites W1848221755 @default.
• W2103245112 cites W1981582689 @default.
• W2103245112 cites W1992603221 @default.
• W2103245112 cites W1999165211 @default.
• W2103245112 cites W2005986251 @default.
• W2103245112 cites W2013257494 @default.
• W2103245112 cites W2024741426 @default.
• W2103245112 cites W2031549483 @default.
• W2103245112 cites W2035084105 @default.
• W2103245112 cites W2049476833 @default.
• W2103245112 cites W2065472386 @default.
• W2103245112 cites W2068791200 @default.
• W2103245112 cites W2079467901 @default.
• W2103245112 cites W2080596545 @default.
• W2103245112 cites W2088400573 @default.
• W2103245112 cites W2095891762 @default.
• W2103245112 cites W2099464226 @default.
• W2103245112 cites W2115970730 @default.
• W2103245112 cites W4213114154 @default.
• W2103245112 cites W4236263205 @default.
• W2103245112 cites W4254726954 @default.
• W2103245112 doi "https://doi.org/10.1016/s0141-8130(98)00009-9" @default.
• W2103245112 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9644594" @default.
• W2103245112 hasPublicationYear "1998" @default.
• W2103245112 type Work @default.
• W2103245112 sameAs 2103245112 @default.
• W2103245112 citedByCount "18" @default.
• W2103245112 countsByYear W21032451122016 @default.
• W2103245112 countsByYear W21032451122017 @default.
• W2103245112 countsByYear W21032451122019 @default.
• W2103245112 crossrefType "journal-article" @default.
• W2103245112 hasAuthorship W2103245112A5003973944 @default.
• W2103245112 hasAuthorship W2103245112A5058346480 @default.
• W2103245112 hasAuthorship W2103245112A5071985859 @default.
• W2103245112 hasAuthorship W2103245112A5087157615 @default.
• W2103245112 hasConcept C104292427 @default.
• W2103245112 hasConcept C104317684 @default.
• W2103245112 hasConcept C12554922 @default.
• W2103245112 hasConcept C133571119 @default.
• W2103245112 hasConcept C13965031 @default.
• W2103245112 hasConcept C181199279 @default.
• W2103245112 hasConcept C185592680 @default.
• W2103245112 hasConcept C202878990 @default.
• W2103245112 hasConcept C204328495 @default.
• W2103245112 hasConcept C2776441376 @default.
• W2103245112 hasConcept C2776923230 @default.
• W2103245112 hasConcept C2779463914 @default.
• W2103245112 hasConcept C547475151 @default.
• W2103245112 hasConcept C55493867 @default.
• W2103245112 hasConcept C8010536 @default.
• W2103245112 hasConcept C86803240 @default.
• W2103245112 hasConceptScore W2103245112C104292427 @default.
• W2103245112 hasConceptScore W2103245112C104317684 @default.
• W2103245112 hasConceptScore W2103245112C12554922 @default.
• W2103245112 hasConceptScore W2103245112C133571119 @default.
• W2103245112 hasConceptScore W2103245112C13965031 @default.
• W2103245112 hasConceptScore W2103245112C181199279 @default.
• W2103245112 hasConceptScore W2103245112C185592680 @default.
• W2103245112 hasConceptScore W2103245112C202878990 @default.
• W2103245112 hasConceptScore W2103245112C204328495 @default.
• W2103245112 hasConceptScore W2103245112C2776441376 @default.
• W2103245112 hasConceptScore W2103245112C2776923230 @default.
• W2103245112 hasConceptScore W2103245112C2779463914 @default.
• W2103245112 hasConceptScore W2103245112C547475151 @default.
• W2103245112 hasConceptScore W2103245112C55493867 @default.
• W2103245112 hasConceptScore W2103245112C8010536 @default.
• W2103245112 hasConceptScore W2103245112C86803240 @default.
• W2103245112 hasIssue "1" @default.
• W2103245112 hasLocation W21032451121 @default.
• W2103245112 hasLocation W21032451122 @default.
• W2103245112 hasOpenAccess W2103245112 @default.
• W2103245112 hasPrimaryLocation W21032451121 @default.
• W2103245112 hasRelatedWork W1964066260 @default.
• W2103245112 hasRelatedWork W1976696191 @default.
• W2103245112 hasRelatedWork W2031549483 @default.
• W2103245112 hasRelatedWork W2057183688 @default.
• W2103245112 hasRelatedWork W2071616396 @default.
• W2103245112 hasRelatedWork W2090595225 @default.
• W2103245112 hasRelatedWork W2099572354 @default.
• W2103245112 hasRelatedWork W2103245112 @default.

• next