The role of the N-terminal domain of T4 gene 32 protein in the cooperatively bound protein - single-stranded nucleic acid complex /
a possible kinetic defect in cooperative binding by the B-
| Main Author: | |
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| Format: | Thesis Book |
| Language: | English |
| Published: |
[Place of publication not identified] :
[publisher not identified] ;
1995.
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| Subjects: | |
| Online Access: | http://proxy.library.tamu.edu/login?url=http://proquest.umi.com/pqdweb?did=742745221&sid=1&Fmt=2&clientId=2945&RQT=309&VName=PQD Link to OAKTrust copy |
| Summary: | a possible kinetic defect in cooperative binding by the B- ability of the mutant protein to bind the pairing substrate. accounted for by a simple loss of binding affinity suggesting acids by gp32. However, previous characterization of the complexes in a functionally significant manner. More concentration was assessed and compared to the ability of the conditions reveal significantly shorter lifetimes of mutant cooperative gp32-ssDNA complex. domain mutants, R4K, R4Q, R4T, R4G, and K3A to poly(A) are domain mutants. Fluorescence stopped-flow kinetic equilibrium binding properties of wild-type (wt), and five B- gp32 to ss nucleic acids which state that only cooperativity highly cooperative binding to single-stranded (ss) nucleic importantly, correlation of kinetic and equilibrium binding inconsistent with simple models of cooperative binding by less in most cases for the B-domain mutants than could be measurements of the NaCi-induced rate of dissociation from modulates the kinetic stability of cooperative gp32-ssDNA mutant proteins to saturate the homologous pairing substrate, mutant, the ability of the proteins to stimulate the in vitro mutants were found to bind cooperatively to ss nucleic acids, poly(A) for R4K, R4Q, and K3A gp32s over a range of solution protein-nucleic complexes suggesting that the B-domain results for these mutant proteins allow us for the first time should be affected by mutations in this domain. All five significant dependence of the functional efficiency on the ssMl3mpl9 DNA under the same conditions. Results indicate a The N-terminal 21 amino acids ("B"-domain) are essential for to assign a functional role to the B-domain of gp32 in the To further determine the nature of the deficiencies in each uvsx-catalyzed homologous pairing assay as a function of gp32 with Kint affected significantly in all but the R4K mutant. Yet, levels of stimulation in the pairing assay were still |
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| Item Description: | "Major Subject: Biochemistry". In title, numerals are used. Vita. |
| Physical Description: | xv, 178 leaves : illustrations ; 28 cm. Issued also on microfiche from University Microfilms Inc. |
| Bibliography: | Includes bibliographical references. |