Characterization of versatile temperature-sensitive magnetic semiconductor with nonlinear negative resistance

1987 ◽  
Vol 107 (3) ◽  
pp. 14-20
Author(s):  
Kyoshiro Seki ◽  
Jun-Ichi Shida ◽  
Koichi Murakami
Keyword(s):  
Magnetic Semiconductor ◽  
Negative Resistance ◽  
Temperature Sensitive

scholarly journals Characterization of Mmp37p, aSaccharomyces cerevisiaeMitochondrial Matrix Protein with a Role in Mitochondrial Protein Import

2006 ◽  
Vol 17 (9) ◽  
pp. 4051-4062 ◽  
Author(s):  
Michelle R. Gallas ◽  
Mary K. Dienhart ◽  
Rosemary A. Stuart ◽  
Roy M. Long
Keyword(s):  
Matrix Protein ◽  
Protein Import ◽  
Mitochondrial Protein ◽  
Temperature Sensitive ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Close Proximity ◽  
The Matrix ◽  
Targeting Signal

Many mitochondrial proteins are encoded by nuclear genes and after translation in the cytoplasm are imported via translocases in the outer and inner membranes, the TOM and TIM complexes, respectively. Here, we report the characterization of the mitochondrial protein, Mmp37p (YGR046w) and demonstrate its involvement in the process of protein import into mitochondria. Haploid cells deleted of MMP37 are viable but display a temperature-sensitive growth phenotype and are inviable in the absence of mitochondrial DNA. Mmp37p is located in the mitochondrial matrix where it is peripherally associated with the inner membrane. We show that Mmp37p has a role in the translocation of proteins across the mitochondrial inner membrane via the TIM23-PAM complex and further demonstrate that substrates containing a tightly folded domain in close proximity to their mitochondrial targeting sequences display a particular dependency on Mmp37p for mitochondrial import. Prior unfolding of the preprotein, or extension of the region between the targeting signal and the tightly folded domain, relieves their dependency for Mmp37p. Furthermore, evidence is presented to show that Mmp37 may affect the assembly state of the TIM23 complex. On the basis of these findings, we hypothesize that the presence of Mmp37p enhances the early stages of the TIM23 matrix import pathway to ensure engagement of incoming preproteins with the mtHsp70p/PAM complex, a step that is necessary to drive the unfolding and complete translocation of the preprotein into the matrix.

Biochemical characterization of poliovirus type 1 temperature-sensitive mutants

Virology ◽  
1984 ◽  
Vol 139 (2) ◽  
pp. 403-407 ◽  
Author(s):  
Christine Bellocq ◽  
Henri Agut ◽  
Sylvie Van Der Werf ◽  
Marc Girard
Keyword(s):  
Biochemical Characterization ◽  
Temperature Sensitive ◽  
Poliovirus Type ◽  
Temperature Sensitive Mutants
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