Inverse relationship of cotranslational translocation with the hydrophobic moment of the bovine preproparathyroid hormone signal sequence.
To investigate the dependence of transmembrane translocation on the hydrophobic moment of the hydrophobic core of the preproparathyroid hormone signal sequence, amino acids were switched to maximize or minimize the hydrophobic moment without changing the length or overall hydrophobicity of the core. As assayed in an in vitro translation system with microsomal membranes, the efficiency of translocation of these mutants was inversely related to the hydrophobic moment, indicating the hydrophobic moment or a related property may contribute to translocational activity.
Ahn
K
K
Department of Physiology and Biophysics, University of Illinois at Urbana-Champaign 61801.
Chen
D
D
Kemper
B
B
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D008969:Molecular Sequence Data; D010281:Parathyroid Hormone / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D011498:Protein Precursors / Q000235:genetics / Q000378:metabolism*; D021382:Protein Sorting Signals / Q000235:genetics / Q000378:metabolism*
D010281:Parathyroid Hormone; D011498:Protein Precursors; D021382:Protein Sorting Signals; C019056:preproparathormone