Structural requirements for α‐mating factor activity
Structural requirements for α‐mating factor activity
复制标题
α交配因子活性的结构要求
DOI:
10.1016/0014-5793(96)00726-0
复制
发表时间:
1996
期刊:
影响因子:
3.5
通讯作者:
C. Flanagan
中科院分区:
文献类型:
--
作者:
G. Houen;O. Nielsen;C. Flanagan
The sexual hormone of S. cerevisiae, α-mating factor (α-MF, WHWLQLKPGQPMY) has structural homology with mammalian luteinizing hormone releasing hormone (LHRH, pEHWSYGLRPG-NH2) and has been shown to exhibit LHRH activity [Loumaye et al. (1982) Science 218, 1323–1325]. We have tested whether LHRH has α-MF activity in yeast and found that it does not. We therefore synthesized a series of hybrid peptides of α-MF and LHRH to study the structural features which determine α-MF and LHRH activities. A hybrid peptide consisting of the LHRH sequence with the C-terminal tetrapeptide (QPMY) of α-MF did not exhibit α-MF activity. Thus, the lack of α-MF activity of LHRH is not due solely to the absence of the C-terminal residues. Substitution of Lys7in α-MF with Arg, as is found in LHRH, did not affect the α-MF activity, nor did an additional substitution of Trp1with pGlu. However, the C-terminal four amino acids of α-MF were necessary for α-MF activity. Our results indicate that insertion of a Ser residue in position 4 as found in LHRH abolishes α-MF activity. These results suggest that, in addition to an intact C-terminus correct spacing of the N-terminal His2and the C-terminus is required for α-MF activity. The hybrid peptides all exhibited less LHRH activity than either LHRH or α-MF. These structure-function studies indicate that the structural homology between these two reproductive hormones may not reflect an evolutionary relationship between them.
影响因子:
9.7
作者:
Fekete,M;Zalatnai,A;Schally,AV
通讯作者:
Schally,AV
DOI:
10.1073/pnas.88.6.2244
发表时间:
1991
影响因子:
11.1
作者:
Liebow,C;Lee,MT;Kamer,AR;Schally,AV
通讯作者:
Schally,AV