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928 Aktuelle Fachpublikationen von Proceedings of the National Academy of Sciences

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Genetically encoded sensors of protein hydrodynamics and molecular proximity [Biochemistry]

19.05.2015 | Alexander C. Hoepker; Ariel Wang; Alix Le Marois; Klaus Suhling; Yuling Yan; Gerard Marriott, Proceedings of the National Academy of Sciences current issue, 2015

The specialized light organ of the ponyfish supports the growth of the bioluminescent symbiont Photobacterium leiognathi. The bioluminescence of P. leiognathi is generated within a heteromeric protein complex composed of the bacterial luciferase and a 20-kDa lumazine binding protein (LUMP), which ...

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Lester Reed: A "complex" man who loved science [Retrospectives]

19.05.2015 | Marvin L. Hackert; Dean R. Appling; Alan M. Lambowitz, Proceedings of the National Academy of Sciences current issue, 2015

Lester J. Reed, a pioneer in the field of biochemistry, died peacefully in Austin, Texas on January 14, 2015 at the age of 90. Lester Reed was born in New Orleans on January 3, 1925. He showed an early interest in chemistry, having his own laboratory in a shed under...

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Activation of the bacterial thermosensor DesK involves a serine zipper dimerization motif that is modulated by bilayer thickness [Biochemistry]

19.05.2015 | Larisa Estefanía Cybulski; Joost Ballering; Anastassiia Moussatova; Maria Eugenia Inda; Daniela B. Vazquez; Tsjerk A ..., Proceedings of the National Academy of Sciences current issue, 2015

DesK is a bacterial thermosensor protein involved in maintaining membrane fluidity in response to changes in environmental temperature. Most likely, the protein is activated by changes in membrane thickness, but the molecular mechanism of sensing and signaling is still poorly understood. Here we ...

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Correction for Kaushal et al., Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome [Correction]

19.05.2015 | Proceedings of the National Academy of Sciences current issue, 2015

BIOCHEMISTRY Correction for “Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome,” by Prem S. Kaushal, Manjuli R. Sharma, Timothy M. Booth, Emdadul M. Haque, Chang-Shung Tung, Karissa Y. Sanbonmatsu, Linda L. Spremulli, and Rajendra K. Agrawal, which appeared in issue ...

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Nonsense suppression in archaea [Biochemistry]

12.05.2015 | Arpita Bhattacharya; Caroline Köhrer; Debabrata Mandal; Uttam L. RajBhandary, Proceedings of the National Academy of Sciences current issue, 2015

Bacterial strains carrying nonsense suppressor tRNA genes played a crucial role in early work on bacterial and bacterial viral genetics. In eukaryotes as well, suppressor tRNAs have played important roles in the genetic analysis of yeast and worms. Surprisingly, little is known about genetic ...

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How release of phosphate from mammalian F1-ATPase generates a rotary substep [Biochemistry]

12.05.2015 | John V. Bason; Martin G. Montgomery; Andrew G. W. Leslie; John E. Walker, Proceedings of the National Academy of Sciences current issue, 2015

The rotation of the central stalk of F1-ATPase is driven by energy derived from the sequential binding of an ATP molecule to its three catalytic sites and the release of the products of hydrolysis. In human F1-ATPase, each 360° rotation consists of three 120° steps composed of substeps of about...

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A site of varicella-zoster virus vulnerability identified by structural studies of neutralizing antibodies bound to the glycoprotein complex gHgL [Biochemistry]

12.05.2015 | Yi Xing; Stefan L. Oliver; TuongVi Nguyen; Claudio Ciferri; Avishek Nandi; Julie Hickman; Cinzia Giovani; Edward Yan ..., Proceedings of the National Academy of Sciences current issue, 2015

Varicella-zoster virus (VZV), of the family Alphaherpesvirinae, causes varicella in children and young adults, potentially leading to herpes zoster later in life on reactivation from latency. The conserved herpesvirus glycoprotein gB and the heterodimer gHgL mediate virion envelope fusion with ...

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Crystal structure of the human mitochondrial chaperonin symmetrical football complex [Biochemistry]

12.05.2015 | Shahar Nisemblat; Oren Yaniv; Avital Parnas; Felix Frolow; Abdussalam Azem, Proceedings of the National Academy of Sciences current issue, 2015

Human mitochondria harbor a single type I chaperonin system that is generally thought to function via a unique single-ring intermediate. To date, no crystal structure has been published for any mammalian type I chaperonin complex. In this study, we describe the crystal structure of a ...

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Major reorientation of tRNA substrates defines specificity of dihydrouridine synthases [Biochemistry]

12.05.2015 | Robert T. Byrne; Huw T. Jenkins; Daniel T. Peters; Fiona Whelan; James Stowell; Naveed Aziz; Pavel Kasatsky; Marina ..., Proceedings of the National Academy of Sciences current issue, 2015

The reduction of specific uridines to dihydrouridine is one of the most common modifications in tRNA. Increased levels of the dihydrouridine modification are associated with cancer. Dihydrouridine synthases (Dus) from different subfamilies selectively reduce distinct uridines, located at ...

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Structural basis of human {gamma}-secretase assembly [Biochemistry]

12.05.2015 | Linfeng Sun; Lingyun Zhao; Guanghui Yang; Chuangye Yan; Rui Zhou; Xiaoyuan Zhou; Tian Xie; Yanyu Zhao; Shenjie Wu; X ..., Proceedings of the National Academy of Sciences current issue, 2015

The four-component intramembrane protease γ-secretase is intricately linked to the development of Alzheimer’s disease. Despite recent structural advances, the transmembrane segments (TMs) of γ-secretase remain to be specifically assigned. Here we report a 3D structure of human γ-secretase at ...

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