High impact information on HSP150

• The COPII components Sec23p and Sec31p and the GTP/GDP exchange factor Sec12p were required in functional form for secretion of Hsp150 [1].
• We show herein that normal function of Sec13p was not required for ER exit of the Hsp150 glycoprotein [1].
• The hsp150 pre-pro-protein consists of a signal peptide, subunit I, a repetitive region, and a unique C terminus [2].
• Our data show that a soluble cargo protein, Hsp150, is selected actively and specifically to budding sites lacking normal Sec24p by a signature residing in its C-terminal domain [3].
• Hsp150 was secreted to the medium in a sec24-1 mutant at restrictive temperature 37 degrees C, while cell wall invertase and vacuolar carboxypeptidase Y remained in the ER [3].

Biological context of HSP150

• The HSP150 mRNA level was increased by nitrogen limitation at 24 degrees C, even when under the control of a HSP150 promoter region of 137 bp carrying the mutagenized HSE [4].
• To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5' deletion derivatives of the HSP150 promoter [4].
• The results for the HSP150 gene suggest that there is an overlap between Al ion stress, oxidative stress and heat shock stress in yeast [5].
• To promote proper folding and secretion competence of this catalytic domain in yeast, it was fused to the Hsp150 delta carrier, which is an N-terminal fragment of a secretory glycoprotein of S. cerevisiae [6].

Anatomical context of HSP150

• Further cell wall analyses demonstrated that Pir2p/Hsp150 and possibly other Pir cell wall proteins, which were already known to be linked to the beta1,3-glucan framework by an alkali-sensitive linkage, were also more efficiently retained in the cell wall at pH 3.5 than at pH 5 [7].
• The hsp150 delta-carrier, which is an N-terminal fragmented of a natural secretory protein of yeast, is able to confer secretion-competence to several heterologous proteins, which otherwise remain in the yeast endoplasmic reticulum [8].

Associations of HSP150 with chemical compounds

• Dual regulation by heat and nutrient stress of the yeast HSP150 gene encoding a secretory glycoprotein [4].
• Protective roles of two aluminum (Al)-induced genes, HSP150 and SED1 of Saccharomyces cerevisiae, in Al and oxidative stresses [5].
• Reduction of folded hsp150, accumulated in the ER due to a sec block prior to DTT treatment, did not inhibit its secretion [9].
• The yeast cells were grown in the presence or absence of doxycycline, and both the growth and secretion of the heat shock protein, Hsp150p, into the culture medium were determined [10].
• Here we present evidence that Hsp150/Pir2, a member of the Pir family of cell wall proteins, can be extracted from the purified cell walls of Saccharomyces cerevisiae by treatment with beta-mercaptoethanol, demonstrating that at least part of this protein is attached to the cell wall through disulfide bridges [11].

Other interactions of HSP150

• The expression analysis showed that genes involved in stress response, such as YGP1, TPS1 and HSP150, were induced under the acid shock response [12].
• Using temperature-sensitive sec24-1 mutants, we showed previously that a secretory glycoprotein, Hsp150, does not require functional Sec24p for ER exit [13].
• The Al tests indicated that the HSP150 protein served a basal protective role in Al stress, but SED1 did not; both of the genes had protective roles for oxidative stresses [5].
• The strength of the HSP150 promoter was found to be comparable to that of the GAL1 promoter [14].
• When RER2 was downregulated, cells secreted Hsp150p that was not of the mature size [10].

Analytical, diagnostic and therapeutic context of HSP150

• Northern blot hybridization analysis showed a substantial increase in HSP150 mRNA level after heat shock [15].

References