HSM3 cDNA ORF clone, Saccharomyces cerevisiae S288C

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Complete DNA sequence of yeast chromosome II.
Feldmann H, Aigle M, Aljinovic G, Andr? B, Baclet MC, Barthe C, Baur A, B?cam AM, Biteau N, Boles E, Brandt T, Brendel M, Br?ckner M, Bussereau F, Christiansen C, Contreras R, Crouzet M, Cziepluch C, D?molis N, Delaveau T, Doignon F, Domdey H, D?sterhus S, Dubois E, Dujon B, El Bakkoury M, Entian KD, Feurmann M, Fiers W, Fobo GM, Fritz C, Gassenhuber H, Glandsdorff N, Goffeau A, Grivell LA, de Haan M, Hein C, Herbert CJ, Hollenberg CP, Holmstr?m K, Jacq C, Jacquet M, Jauniaux JC, Jonniaux JL, Kalles?e T, Kiesau P, Kirchrath L, K?tter P, Korol S, Liebl S, Logghe M, Lohan AJ, Louis EJ, Li ZY, Maat MJ, Mallet L, Mannhaupt G, Messenguy F, Miosga T, Molemans F, M?ller S, Nasr F, Obermaier B, Perea J, Pi?rard A, Piravandi E, Pohl FM, Pohl TM, Potier S, Proft M, Purnelle B, Ramezani Rad M, Rieger M, Rose M, Schaaff-Gerstenschl?ger I, Scherens B, Schwarzlose C, Skala J, Slonimski PP, Smits PH, Souciet JL, Steensma HY, Stucka R, Urrestarazu A, van der Aart QJ, van Dyck L, Vassarotti A, Vetter I, Vierendeels F, Vissers S, Wagner G, de Wergifosse P, Wolfe KH, Zagulski M, Zimmermann FK, Mewes HW, Kleine K
The EMBO journal13(24)5795-809(1994 Dec)

Combinations of hsm3 and hsm6 mutations with mutations in other genes of the RAD52 epistatic group did not provide a spontaneous mutation rate decrease.
Title: [Spontaneous mutation rate changes in saccharomyces cerevisiae at combinations of hsm3 and hsm6 mutations with rad52 mutation].

the structural basis of the molecular functions of Hsm3 for the regulatory particle assembly.
Title: Structural basis for specific recognition of Rpt1p, an ATPase subunit of 26 S proteasome, by proteasome-dedicated chaperone Hsm3p.

provide structural and biochemical evidence on how Hsm3/S5b may regulate the 19S RP association to the 20S CP proteasome
Title: Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly.

The results made it possible to assume that the hsm3 mutation destabilizes the D-loop, which is a key substrate of both Rad5- and Rad52-dependent postreplicative repair pathways.
Title: [Interaction of the HSM3 gene with genes initiating homologous recombination repair in yeast Saccharomyces cerevisiae].

Hsm3 protein contains at least two domains; the N-terminal part of the domain is responsible for the proteasome assembly, whereas the C-terminal portion of the protein is responsible for mutagenesis.
Title: [Interaction of gene HSM3 with genes of the epistatic RAD6 group in yeast Saccharomyces cerevisiae].