How NASA’s SPHEREx Mission Will Share Its All-Sky Map With the World

NASA’s SPHEREx mission will map the entire sky in 102 different wavelengths, or colors, of infrared light. This image of the Vela Molecular Ridge was captured by SPHEREx and is part of the mission’s first ever public data release. The yellow patch on the right side of the image is a cloud of interstellar gas and dust that glows in some infrared colors due to radiation from nearby stars.

NASA/JPL-Caltech

NASA’s newest astrophysics space telescope launched in March on a mission to create an all-sky map of the universe. Now settled into low-Earth orbit, SPHEREx (Spectro-Photometer for the History of the Universe, Epoch of Reionization, and Ices Explorer) has begun delivering its sky survey data to a public archive on a weekly basis, allowing anyone to use the data to probe the secrets of the cosmos.

“Because we’re looking at everything in the whole sky, almost every area of astronomy can be addressed by SPHEREx data,” said Rachel Akeson, the lead for the SPHEREx Science Data Center at IPAC. IPAC is a science and data center for astrophysics and planetary science at Caltech in Pasadena, California.

“Almost every area of astronomy can be addressed by SPHEREx data.

Rachel Akeson

SPHEREx Science Data Center Lead

Other missions, like NASA’s now-retired WISE (Wide-field Infrared Survey Explorer), have also mapped the entire sky. SPHEREx builds on this legacy by observing in 102 infrared wavelengths, compared to WISE’s four wavelength bands.

By putting the many wavelength bands of SPHEREx data together, scientists can identify the signatures of specific molecules with a technique known as spectroscopy. The mission’s science team will use this method to study the distribution of frozen water and organic molecules — the “building blocks of life” — in the Milky Way. 

This animation shows how NASA’s SPHEREx observatory will map the entire sky — a process it will complete four times over its two-year mission. The telescope will observe every point in the sky in 102 different infrared wavelengths, more than any other all-sky survey. SPHEREx’s openly available data will enable a wide variety of astronomical studies. Credit: NASA/JPL-Caltech

The SPHEREx science team will also use the mission’s data to study the physics that drove the universe’s expansion following the big bang, and to measure the amount of light emitted by all the galaxies in the universe over time. Releasing SPHEREx data in a public archive encourages far more astronomical studies than the team could do on their own.

“By making the data public, we enable the whole astronomy community to use SPHEREx data to work on all these other areas of science,” Akeson said.

NASA is committed to the sharing of scientific data, promoting transparency and efficiency in scientific research. In line with this commitment, data from SPHEREx appears in the public archive within 60 days after the telescope collects each observation. The short delay allows the SPHEREx team to process the raw data to remove or flag artifacts, account for detector effects, and align the images to the correct astronomical coordinates.

The team publishes the procedures they used to process the data alongside the actual data products. “We want enough information in those files that people can do their own research,” Akeson said.

During its two-year prime mission, SPHEREx will survey the entire sky twice a year, creating four all-sky maps. After the mission reaches the one-year mark, the team plans to release a map of the whole sky at all 102 wavelengths.

In addition to the science enabled by SPHEREx itself, the telescope unlocks an even greater range of astronomical studies when paired with other missions. Data from SPHEREx can be used to identify interesting targets for further study by NASA’s James Webb Space Telescope, refine exoplanet parameters collected from NASA’s TESS (Transiting Exoplanet Survey Satellite), and study the properties of dark matter and dark energy along with ESA’s (European Space Agency’s) Euclid mission and NASA’s upcoming Nancy Grace Roman Space Telescope.

The SPHEREx mission’s all-sky survey will complement data from other NASA space telescopes. SPHEREx is illustrated second from the right. The other telescope illustrations are, from left to right: the Hubble Space Telescope, the retired Spitzer Space Telescope, the retired WISE/NEOWISE mission, the James Webb Space Telescope, and the upcoming Nancy Grace Roman Space Telescope.

NASA/JPL-Caltech

The IPAC archive that hosts SPHEREx data, IRSA (NASA/IPAC Infrared Science Archive), also hosts pointed observations and all-sky maps at a variety of wavelengths from previous missions. The large amount of data available through IRSA gives users a comprehensive view of the astronomical objects they want to study.

“SPHEREx is part of the entire legacy of NASA space surveys,” said IRSA Science Lead Vandana Desai. “People are going to use the data in all kinds of ways that we can't imagine.”

NASA's Office of the Chief Science Data Officer leads open science efforts for the agency. Public sharing of scientific data, tools, research, and software maximizes the impact of NASA’s science missions. To learn more about NASA’s commitment to transparency and reproducibility of scientific research, visit science.nasa.gov/open-science. To get more stories about the impact of NASA’s science data delivered directly to your inbox, sign up for the NASA Open Science newsletter.

By Lauren Leese
Web Content Strategist for the Office of the Chief Science Data Officer  

Source: How NASA’s SPHEREx Mission Will Share Its All-Sky Map With the World  - NASA Science

Uncovering the mechanism behind dual-end cleavage in transfer RNAs - Biology Biotechnology - Molecular & Computational biology

Star-shaped small enzyme with "dual-functionality" helps in proper tRNA functioning. HARPs are the smallest known RNase P enzymes that help with tRNA maturation in bacteria and archaea. How such a small enzyme accomplishes this crucial task has baffled researchers for some time. Now, researchers from Kyushu University, Japan, have revealed that HARPs form a 12-subunit star-shaped structure with binding sites to process both the ends (5' and 3') of pre-tRNAs. This novel observation, where small enzymes take up different forms to perform multiple functions, suggests molecular evolution of these crucial enzymes. Credit: Takamasa Teramoto/Yoshimitsu Kakuta/Kyushu University

To build proteins, cells rely on a molecule called transfer RNA, or tRNA. tRNAs act like protein-building couriers, where they read the genetic instructions from messenger RNA, mRNA, and deliver the right amino acids to ribosomes, the cell's protein-making factories. But before tRNAs can do their work, they first need to be trimmed and shaped properly.

Now, researchers from Kyushu University have revealed that the smallest known protein-based tRNA-processing enzyme, called HARP, forms a star-shaped complex of 12 protein molecules, making it capable of cutting both the 5' and 3' ends of tRNA. The team hopes that their findings will have a broad impact on synthetic biology and biotechnology research, and aid in the designing of artificial enzymes and RNA processing tools. Their findings were published in the journal Nature Communications.

In any biological system, most proteins that are made in the cell need to undergo processing for them to fully work. In the case of tRNA, one of those processes is the cutting of the straggling ends of the RNA that make up the molecule. Depending on the direction, these are called 5-prime or 3-prime ends, denoted as 5' and 3', respectively.

One key enzyme responsible for cutting the extra segment at the 5' end of the tRNA is RNase P. Found in almost all life forms, this enzyme exists in two broad forms: one that is mostly made of RNA and another that is entirely protein-based. The RNA-based version usually forms a large, complex structure with several proteins and has been well studied over the past 40 years. 

Overall view of five pre-tRNA binding by HARP dodecamer. Credit: Nature Communications (2025). DOI: 10.1038/s41467-025-60002-1

On the other hand, protein-only RNase P enzymes are more streamlined. These come in two main types: PRORP, which is found in higher organisms like plants and animals, and HARP, which is found in certain bacteria and archaea. HARP—short for Homologs of Aquifex RNase P36—is known for its small size and unique six-pointed, star-like structure. But how it performs such a complex task—or why it forms such a distinctive shape—remained unclear.

"To investigate and visualize HARP bound to pre-tRNA and uncover how it processes the molecule, we used cryogenic electron microscopy (cryo-EM) single-particle analysis," explains Professor Yoshimitsu Kakuta from Kyushu University's Faculty of Agriculture, who led the study.

The researchers found that the overall structure of the enzyme with the pre-tRNAs had a radial structure with pre-tRNA molecules alternately bound to five binding sites on the enzyme. Cryo-EM analysis showed that the 12-subunit HARP enzyme acts like a "molecular ruler," measuring the distance from the 5' end to the "elbow" of the pre-tRNA to precisely identify the cleavage site. Remarkably, this mechanism was also observed in other types of RNase P enzymes, indicating a case of convergent evolution across different organisms.

Architectural diversity of RNase P enzymes and their common concept of substrate recognition. Credit: Nature Communications (2025). DOI: 10.1038/s41467-025-60002-1

"Our structural analysis shed light on how HARP processes the 5' leader sequence and revealed that the functional 12-subunit HARP complex binds only five pre-tRNA molecules, not ten as previously predicted," adds Assistant Professor Takamasa Teramoto, the first author of the study. "This means that 7 of the enzyme's 12 active sites remain unoccupied."

When the team conducted cleavage assays to understand the functionality of these vacant sites, they found a second cleavage product that corresponded to the 3' end of the pre-tRNA. This was a new finding. It suggests that HARPs first trim the extra nucleotides at the 5' end and then use the remaining empty active sites to carry out the cleavage at the 3' end.

"The oligomerization of the small protein HARP confers it with bifunctionality in pre-tRNA processing. Our findings illustrate an evolutionary strategy by which organisms with compact genomes can acquire multifunctionality," concludes Kakuta.

Uncovering such evolutionary strategies where limited structural elements are arranged flexibly to gain new functions could assist in the development of future tools in synthetic biology and biotechnology. 

by Kyushu University

edited by Gaby Clark, reviewed by Robert Egan 

Source: Uncovering the mechanism behind dual-end cleavage in transfer RNAs