TY - JOUR
T1 - CADp44
T2 - A novel regulatory subunit of the 26S proteasome and the mammalian homolog of yeast Sug2p
AU - Bauer, Vernon W.
AU - Swaffield, Jonathan C.
AU - Johnston, Stephen Albert
AU - Andrews, Matthew T.
N1 - Funding Information:
This manuscript was prepared with the substantial help of Martha Rollins. We thank G. DeMartino, C. Slaughter, and K. Tanaka for communicating their p42 DNA sequence prior to publication, J. Sampson for technical assistance, R. Burlington for help with the capture, care and handling of thirteen-lined ground squirrels and K. Vrana for instruction in various surgical procedures. This work was supported by a grant to M.T.A. from the North Carolina Biotechnology Center (9413-ARG-0034) and a grant to S.A.J. from NIH.
PY - 1996/11/28
Y1 - 1996/11/28
N2 - We have identified a novel protein, CADp44, based on the analysis of cDNAs derived from the brainstem of the 13-lined ground squirrel, Spermophilus tridecemlineatus. CADp44 has an unmodified molecular mass of 44,178 Da and contains multiple functional domains, including a conserved ATPase domain (CAD) and a leucine zipper motif. We show that distinct regions of the CADp44 sequence are identical to a set of peptides prepared from a recently identified bovine protein, referred to as p42, which is found in the PA700 regulatory complex of the 26S proteasome. We also show that CADp44 is the functional homolog of the newly characterized Sug2 protein from the budding yeast, Saccharomyces cerevisiae. Consistent with its role as a component of the 26S proteasome, CADp44 mRNA is found in all ground squirrel tissues examined. Evolutionary relationships based on sequence analysis show that both CADp44 and yeast Sug2p are distinct from the other five CAD ATPases found in the PA700, and together comprise the sixth and newest CAD subunit of the regulatory complex of the 26S proteasome.
AB - We have identified a novel protein, CADp44, based on the analysis of cDNAs derived from the brainstem of the 13-lined ground squirrel, Spermophilus tridecemlineatus. CADp44 has an unmodified molecular mass of 44,178 Da and contains multiple functional domains, including a conserved ATPase domain (CAD) and a leucine zipper motif. We show that distinct regions of the CADp44 sequence are identical to a set of peptides prepared from a recently identified bovine protein, referred to as p42, which is found in the PA700 regulatory complex of the 26S proteasome. We also show that CADp44 is the functional homolog of the newly characterized Sug2 protein from the budding yeast, Saccharomyces cerevisiae. Consistent with its role as a component of the 26S proteasome, CADp44 mRNA is found in all ground squirrel tissues examined. Evolutionary relationships based on sequence analysis show that both CADp44 and yeast Sug2p are distinct from the other five CAD ATPases found in the PA700, and together comprise the sixth and newest CAD subunit of the regulatory complex of the 26S proteasome.
KW - 26S proteasome
KW - CADp44
KW - Spermophilus
KW - Yeast Sug2p
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U2 - 10.1016/S0378-1119(96)00463-5
DO - 10.1016/S0378-1119(96)00463-5
M3 - Article
C2 - 8973309
AN - SCOPUS:0041175168
SN - 0378-1119
VL - 181
SP - 63
EP - 69
JO - Gene
JF - Gene
IS - 1-2
ER -