• No results found

The BRCT domain from the large subunit of human Replication Factor C

N/A
N/A
Protected

Academic year: 2021

Share "The BRCT domain from the large subunit of human Replication Factor C"

Copied!
7
0
0

Bezig met laden.... (Bekijk nu de volledige tekst)

Hele tekst

(1)

The BRCT domain from the large subunit of human Replication Factor

C

Kobayashi, Masakazu

Citation

Kobayashi, M. (2006, September 6). The BRCT domain from the large subunit of human

Replication Factor C. Retrieved from https://hdl.handle.net/1887/4546

Version: Corrected Publisher’s Version

(2)

The BRCT domain from the large subunit of

human Replication Factor C: Protein-DNA

complex determined by NMR and mutagenesis.

PROEFSCHRIFT

TER VERKRIJGING VAN DE GRAAD VAN DOCTOR AAN DE UNIVERSITEIT LEIDEN, OP GEZAG VAN DE RECTOR MAGNIFICUS DR. D. D. BREIMER, HOOGLERAAR IN DE FACULTEIT DER WISKUNDE EN NATUURWETENSCHAPPEN EN DIE DER GENEESKUNDE, VOLGENS BESLUIT VAN HET COLLEGE VOOR PROMOTIES TE VERDEDIGEN OP WOENSDAG 6 SEPTEMBER 2006 TE KLOKKE 16:15 UUR

Door

Masakazu Kobayashi

(3)

Promotie commissie

Promotor : Prof. Dr. G.W. Canters Co-Promoter: Dr. G. Siegal

Referent : Prof. Dr. P. M. Burgers Overige Leden :

Prof. Dr. J. Brouwer Prof. Dr. R. Boelens

(4)
(5)

Front and rear covers: The layout was designed by Emanuela Lonardi using the original

(6)

Contents

Chapter 1 General Introduction 7

Chapter 2 Characterization of the DNA binding and Structural Properties of the BRCT region of the p140 subunit of human replication Factor C

39

Chapter 3 Amino acid determinants for DNA binding by the BRCT region of human RFC p140

65

Chapter 4 1H,15N and 13C resonance assignments and secondary structure determination of the BRCT Region of the large subunit of human Replication Factor C, bound to DNA

81

Chapter 5 Structure of the BRCT domain from RFC p140: A model Protein-DNA complex determined by NMR and mutagenesis data

93

Chapter 6 General discussions and future prospective 133

Summary in English 143

Samenvatting 146

Appendices: Colour figures 148

List of publications 155

Curriculum Vitae 156

(7)

Referenties

GERELATEERDE DOCUMENTEN

The crystal structure of the complex of the BRCA1 tandem BRCT repeat with a phosphoserine peptide shows that the phosphate moiety of the bound peptide is hydrogen-bonded to the

The later discovery of specialized polymerases that can replicate past lesions resulted in a renaming of this mechanism to DNA Translesion Synthesis

BRCT BRCA1 C-Terminal Domain CIP Calf Intestinal Phosphatase CPD Cyclobutane Pyrimidine Dimer DTD Deoxycytidyl Transferase Domain EMSA Electrophoretic Mobility Shift Assay

The replacement of several amino acids of the BRCT region using site-directed mutagenesis revealed a requirement for not only the few highly conserved aminoc acids, but also

Door lokaal aminozuren te vervangen door andere aminozuren kan er gekeken worden welke residuen uit de BRCT regio van RFC essentieel zijn voor binding van DNA (Hoofdstuk 3).. Door

(B) Surface accessible residues that are conserved (defined in Figure 3.1) are colored with blue onto the structure of p140 (375-480).. N440 is not a

(2006) Characterization of the DNA binding and structural properties of the BRCT region of human replication factor C p140 subunit.. Solution structure

The BRCT domain from the large subunit of human Replication factor C: Protein-DNA complex determined by NMR and mutagenesis. 1) The N-terminal region of the large subunit of RFC