Self-similarities in the frequency-amplitude space of a loss-modulated CO2_2 laser

We show the standard two-level continuous-time model of loss-modulated CO$_2$ lasers to display the same regular network of self-similar stability islands known so far to be typically present only in discrete-time models based on mappings. For class B laser models our results suggest that, more than just convenient surrogates, discrete mappings in fact could be isomorphic to continuous flows.Comment: (5 low-res color figs; for ALL figures high-res PDF: http://www.if.ufrgs.br/~jgallas/jg_papers.html

Accumulation horizons and period-adding in optically injected semiconductor lasers

We study the hierarchical structuring of islands of stable periodic oscillations inside chaotic regions in phase diagrams of single-mode semiconductor lasers with optical injection. Phase diagrams display remarkable {\it accumulation horizons}: boundaries formed by the accumulation of infinite cascades of self-similar islands of periodic solutions of ever-increasing period. Each cascade follows a specific period-adding route. The riddling of chaotic laser phases by such networks of periodic solutions may compromise applications operating with chaotic signals such as e.g. secure communications.Comment: 4 pages, 4 figures, laser phase diagrams, to appear in Phys. Rev. E, vol. 7

Characterization of Mmp37p, a \u3cem\u3eSaccharomyces cerevisiae\u3c/em\u3e Mitochondrial Matrix Protein with a Role in Mitochondrial Protein Import

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