Sld3 is conserved in yeast and fungi, and treslin, also known as Ticrr, has been identified as the functional counterpart of Sld3 in metazoans. However, they differ in size and amino acid sequence. Yeast Sld3 and its metazoan counterpart treslin are ...
Sld3 is conserved in yeast and fungi, and treslin, also known as Ticrr, has been identified as the functional counterpart of Sld3 in metazoans. However, they differ in size and amino acid sequence. Yeast Sld3 and its metazoan counterpart treslin are the hub proteins mediating protein associations critical for formation of the helicase. This entry represents the N-terminal domain of Sld3 which is shown to bind to the N-terminal domain of Sld7 [1,2]. This domain adopts a Ku70-like beta-barrel fold which in Sld3 is truncated, containing five beta-strands [2].
Mitochondrial morphogenesis protein SLD7 N-terminal domain
The initiation of eukaryotic chromosomal DNA replication requires the formation of an active replicative helicase at the replication origins of chromosomes. Yeast Sld3 and its metazoan counterpart treslin are the hub proteins mediating protein associ ...
The initiation of eukaryotic chromosomal DNA replication requires the formation of an active replicative helicase at the replication origins of chromosomes. Yeast Sld3 and its metazoan counterpart treslin are the hub proteins mediating protein associations critical for formation of the helicase. The Sld7 protein interacts with Sld3, and the complex formed is thought to regulate the function of Sld3. Although Sld7 is a non-essential DNA replication protein that is found in only a limited range of yeasts, its depletion slowed the growth of cells and caused a delay in the S phase. Structure analysis indicates that the N-terminal domain of Sld7 binds to the N-terminal region of Sld3 [1].