Rice at the University of Biological Physics is the theory of new cellular mechanics, which seals are truly.

José Onuchic's Rice Laboratory determines the structure of the condensation protein complex. The work decides whether the complex one seal that lassos two double strands of DNA or a molecular "handcuff" consists of two connected rings that each wrangle double strand.

The team led Rice postdoctoral researcher Knife Krepel used to suit state-of-the-art analysis tools to call: this one seal.

The first step in their work is to understand proteins activity on the structure of chromosomes, including all stages of mitochondria and cell life cycles. This understanding will help scientists learn how to better treat genetic diseases, including cancer.

Results of a two-year study of Rice's team will appear Works of the National Academy of Sciences.

Condensin does what the word suggests: it promotes the concentration of chromosomes in the cell nucleus. Recent studies have shown that Condensin and its protein partner Kozine have been exposed to DNA. But to this day, no one has ever decided how to match the functional forms of condensin proteins.

Krepel has begun its analysis of the bacterial capendine complexes of five subdivisions, including two chromosomes (SMC) proteins, which look like each other like hinge and long kleisin proteins that form the rest of the seal. Complexes in the eukaryous nuclei of humans – the target of future analysis – is similar to their archaic counterparts.

Crapple puzzle combines and combines the existing data on the atomic structures and the genetic sequence of individual proteins. Structures have made X-ray crystallizers of protein fragments, and consistent information through direct connection analysis (DCA), published by Onuchic and his colleagues in 2011, comparing amino acids containing proteins.

"We used DCA for coefficients of amino acids and we had a small bit of protein fragments from experiments," Kremlin said. "It was a good starting point, and then we would have to put together a puzzle, we wanted a full structure and we would have to confront this one or double seal."

They know how the proteins are the only key to develop. "This is a modular mechanism with a lot of proteins," said Rice, a postdoctoral researcher and co-author Michel de Pierro. "One protein is crystalline, but it is difficult to understand the structure of the whole complex, so it is ideal to look at the consent that will enable us to get information on the complex, even if we have no structure."

"The coincidence is mostly about natural selection," added Ryan Chen, a postdoctoral researcher and co-author. "As you get occasional mutations, some interactions need to preserve the maintenance function that complex."

"We look forward to where both these wastes go and match, they are growing together," said Onuchic. "If it creates a mutation and has a bad reaction, the other must pay, ask if you can get this consistent information together with the little crystal structures and determine these giant structures and find out that we can."

The Onuchic Group of Rice's Center for Theoretical Biological Physics (CTBP) has published a series of papers that extend its theories of protein folding into a larger genome. He expressed hope that the ongoing works will eventually be revealed on the mechanisms of Condensin. "It's all about chromosomes," he said. "People know it, but nobody knows how they do it."

Onuchic said studies to others suggest a flexible hinge can help open and close the ring, serving as a gateway that allows DNA strands and outside, the process is also hinted by Rice's research. But without knowing all the molecules in the complex, the function and dynamics are not clear.

"We know that Condensin's complex is involved because if you remove it, the mitosis is not going on," he said. "But nobody understands the mechanism, now we have this structure, we have the first shot to understand molecular details."

Story source:

Materials provided Rice University. Original written by Mike Williams. Note: Edit content for style and length.